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1 dF is a scaffold protein, HydA1 is a natural hydrogenase).
2 ding an actinobacteria-type H2-uptake [NiFe]-hydrogenase.
3 , photosystem II, to the H2 evolving enzyme, hydrogenase.
4  of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase.
5 te the proton reduction activity of a [NiFe] hydrogenase.
6 HypC residues relevant for the maturation of hydrogenase.
7 component of the catalytic H-cluster of FeFe hydrogenase.
8 ic electron transport chain and a plastidial hydrogenase.
9 hydrogen evolution activity of this class of hydrogenase.
10 n between flavodoxin/ferredoxin and the NiFe-hydrogenase.
11 itting electron flow from water oxidation to hydrogenase.
12  assembly of the catalytic H cluster of FeFe hydrogenase.
13 g the assembly line toward functional [NiFe]-hydrogenase.
14 O, thereby providing the carbonyl ligand for hydrogenase.
15  of nickel-containing enzymes such as [NiFe]-hydrogenase.
16 f glycine ends up in the CO ligand of [NiFe]-hydrogenase.
17 it elusive, catalytic intermediate of [NiFe]-hydrogenases.
18 ession but decreased expression of all other hydrogenases.
19 the well-studied dinuclear [FeFe] and [NiFe] hydrogenases.
20 ion emulate components of the active site of hydrogenases.
21                                      E. coli hydrogenase 1 (Hyd-1) is adsorbed on a high surface-area
22 es, that the Ni-C to Ni-L interconversion in Hydrogenase-1 (Hyd-1) from Escherichia coli is a pH-depe
23                                              Hydrogenase-1 (Hyd1) (MSMEG_2262-2263) is well-adapted t
24 ide reacts rapidly with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Escherichia coli) u
25  86% of the H2O produced by Escherichia coli hydrogenase-1 exposed to a mixture of 90% H2 and 10% O2
26 electron entry/exit site in Escherichia coli hydrogenase-1 is shown to play a vital role in tuning bi
27                      Escherichia coli uptake hydrogenase 2 (Hyd-2) catalyzes the reversible oxidation
28  with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Escherichia coli) under mild oxidizin
29 y that allows synthesizing functional [NiFe]-hydrogenase-2 of Escherichia coli from purified componen
30 he biosynthesis of the active site of [NiFe]-hydrogenases, a family of H2-activating enzymes.
31                                              Hydrogenase accessory proteins from bacteria-synthesizin
32 t the organometallic component of the [FeFe]-hydrogenase active site (the H-cluster).
33 terfly shape of the 2Fe2S core of the [FeFe]-hydrogenase active site but with nitrosyl rather than ca
34 anting Mu(.) into three models of the [FeFe]-hydrogenase active site we have been able to detect key
35 g in electrocatalysts inspired by the [NiFe]-hydrogenase active site.
36    This reflects either that H/D exchange at hydrogenase active sites is rapid compared to the rate o
37                         As nominal models of hydrogenase active sites, these bimetallics feature two
38                  This highlights the role of hydrogenase activity and PSI-CEF in the ecological succe
39 locality in the chloroplast preserves [FeFe]-hydrogenase activity and supports continuous hydrogen pr
40                     The mutant had no uptake hydrogenase activity but had increased bidirectional hyd
41  cellular compartments, including detectable hydrogenase activity in Mastigamoeba cytosol and mitocho
42     This second assay measures the remaining hydrogenase activity in periodic samples taken from the
43                              At light onset, hydrogenase activity sustains a linear electron flow fro
44 nases, rather than due to the sensitivity of hydrogenase activity to oxygen.
45 e mutant enzyme displayed severely decreased hydrogenase activity.
46 a a periplasmic formate dehydrogenase and/or hydrogenase, allowing energetic coupling to hydrogenotro
47 s as the corresponding cofactors in standard hydrogenases, although their redox potentials are higher
48                  H2 PAD-enabled discovery of hydrogenase and FNR mutants that enhance biological H2 p
49  of S. aciditrophicus and S. wolfei had both hydrogenase and formate dehydrogenase activities.
50         S. aciditrophicus expressed multiple hydrogenase and formate dehydrogenase genes during syntr
51              Both organisms contain multiple hydrogenase and formate dehydrogenase genes, but lack ge
52                 A putative monomeric [Fe-Fe] hydrogenase and Hmc (high-molecular-weight-cytochrome c3
53                   The instability of [Fe-Fe]-hydrogenase and its synthetic models under aerobic condi
54 MBH is encoded by a 14-gene operon with both hydrogenase and Na(+)/H(+) antiporter modules.
55 ch is required for Ni(II) delivery to [NiFe]-hydrogenase and participates in urease maturation.
56 g postulates a direct link between CrPFO and hydrogenase and provides new opportunities to better stu
57 enes involved in the SurR regulon, including hydrogenase and related S(0) -responsive genes.
58                       Transcripts of soluble hydrogenases and ferredoxins from Acetobacterium and hyd
59 I possesses electron transfer flavoproteins, hydrogenases and formate dehydrogenases essential for sy
60 teria, hydrogen evolution is associated with hydrogenases and nitrogenase, making these enzymes inter
61                          Enzymes such as the hydrogenases and nitrogenases are also proposed to invol
62 ntext of the function of the active sites of hydrogenases and nitrogenases.
63  for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.
64 ones, aldehydes, imines, and carbon dioxide, hydrogenases and their model complexes, and palladium ca
65 ures resembling those of O2-sensitive [NiFe] hydrogenases and/or oxidatively damaged protein.
66  of hydride complexes found in nature (e.g., hydrogenases) and in industry (e.g., catalysis and hydro
67 ct metabolic interactions (e.g., periplasmic hydrogenases) and the ratio shift in electron carriers u
68                          Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform cataly
69 oCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and biofuel deve
70 ne gene families involved in photosynthesis, hydrogenases, and proteins involved in defense from envi
71 nal data obtained with various NiFe and FeFe hydrogenases, and we illustrate how the presence of an i
72  oxygen tolerance in soluble, group 3 [NiFe]-hydrogenases, and we present a model integrating both el
73 onic properties of the active site of [NiFe]-hydrogenases are crucial for efficient H2 binding and cl
74                                       [NiFe] hydrogenases are key enzymes for the energy and redox me
75                                       [NiFe] hydrogenases are metalloenzymes that catalyze the revers
76                            Consequently, all hydrogenases are metalloenzymes that contain at least on
77                       Oxygen-tolerant [NiFe] hydrogenases are metalloenzymes that represent valuable
78                                              Hydrogenases are nature's key catalysts involved in both
79                                              Hydrogenases are oxygen-sensitive enzymes that catalyze
80                                       [NiFe]-hydrogenases are redox enzymes composed of a large subun
81  generally accepted that cyanobacterial NiFe-hydrogenases are reduced by NAD(P)H.
82                                       [FeFe]-hydrogenases are the best natural hydrogen-producing enz
83                                         FeFe hydrogenases are the most efficient H2-producing enzymes
84                        Because bidirectional hydrogenases are widespread in aquatic nutrient-rich env
85 active sites of a number of enzymes (such as hydrogenases), are promising therapeutic agents, and hav
86 netic optimization of an artificial transfer hydrogenase (ATHase hereafter), [(eta(5)-Cp*)Ir(pico)Cl]
87 lds an NAD(P)H-dependent artificial transfer hydrogenase (ATHase).
88 n, thus overcoming the O2 sensitivity of the hydrogenase, but its activity is low.
89 cs is recognized for many enzymes, including hydrogenases, but is largely neglected in designing synt
90 he absence of S degrees and have up to seven hydrogenases, but their combined physiological roles are
91 ear active site of an oxygen-tolerant [NiFe] hydrogenase by probing the metal-ligand modes of both th
92 e structure of the active site of the [FeFe] hydrogenases by assembling the active enzyme with a vers
93            Take a breath: An oxygen-tolerant hydrogenase can be employed with a dye in a photocatalyt
94 o study has ever unambiguously proven that a hydrogenase can oxidize this trace gas.
95                                Active [FeFe] hydrogenases can be obtained by expressing the unmaturat
96 sid provides stability and protection to the hydrogenase cargo.
97                                      In FeFe hydrogenases, catalysis occurs at the H cluster, a metal
98                                   The [FeFe]-hydrogenase catalytic site H cluster is a complex iron s
99                                         FeFe hydrogenases catalyze H2 oxidation and formation at an i
100                                       [FeFe] hydrogenases catalyze proton reduction and hydrogen oxid
101                                       [FeFe] hydrogenases catalyze rapid H2 production but are highly
102                                              Hydrogenases catalyze the redox interconversion of proto
103                                   The [FeFe]-hydrogenases catalyze the reversible activation of molec
104                                       [NiFe] hydrogenases catalyze the reversible cleavage of hydroge
105                                         [Fe]-Hydrogenase catalyzes the hydrogenation of a biological
106 ins, is responsible for the synthesis of the hydrogenase CO and CN(-) ligands from tyrosine-derived d
107 gands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligand
108  complex is shown to comprise HycE (a [NiFe] hydrogenase component termed Hyd-3), FdhF (the molybdenu
109 viding rate constants insensitive to initial hydrogenase concentration.
110            The catalytic H-cluster of [FeFe]-hydrogenase consists of a [4Fe-4S] subcluster ([4Fe-4S]H
111                                       [FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster
112        These results may apply to all [FeFe] hydrogenases containing accessory clusters.
113 tral carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cya
114                    The active site of [FeFe] hydrogenase contains a catalytic binuclear iron subsite
115                                              Hydrogenases control the H2-related metabolism in many m
116  and activation in the active site of [NiFe]-hydrogenases could be exploited in the design of novel b
117                                              Hydrogenases couple electrochemical potential to the rev
118 ing the Clostridium pasteurianum (Cp) [FeFe] hydrogenase, CpI, we detected significant rates of direc
119 -cluster of Chlamydomonas reinhardtii [FeFe]-hydrogenase (CrHydA1) affects the H-cluster using electr
120   Experiments were carried out on two [FeFe]-hydrogenases, CrHydA1 from the green alga Chlamydomonas
121                In the case of rod-shaped Cpl hydrogenase crystals, only five crystals and about 30 mi
122 ression of HYDA and the specific activity of hydrogenase demonstrate that C. vulgaris YSL01 and YSL16
123  Mono-iron hydrogenase was the third type of hydrogenase discovered.
124                    Attached to an electrode, hydrogenases display reversible electrocatalytic behavio
125 urthermore, PfSHI, like other group 3 [NiFe]-hydrogenases, does not possess the proximal [4Fe3S] clus
126  is demonstrated for the characterization of hydrogenase during catalytic turnover.
127       We further reveal that group 2a [NiFe] hydrogenases (e.g., Hyd1) can contribute to this process
128 ious studies that have linked group 5 [NiFe] hydrogenases (e.g., Hyd2) to the oxidation of tropospher
129  microelectrodes were modified with a [NiFe]-hydrogenase embedded in a viologen-modified redox hydrog
130 supporting CO2 fixation, as well as a [NiFe] hydrogenase-encoding gene cluster in H2 oxidation.
131 ional model of the active site of the [FeFe] hydrogenase enzyme.
132 ions, including the oxidation of hydrogen by hydrogenase enzymes and ionic hydrogenation of organic c
133 highly express genes encoding group 1 Ni, Fe hydrogenase enzymes for H(2) oxidation.
134                                              Hydrogenase enzymes in nature use hydrogen as a fuel, bu
135    Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors
136                                              Hydrogenase enzymes use Ni and Fe to oxidize H2 at high
137 how the H-H bond is oxidized or generated in hydrogenase enzymes.
138 tion/oxidation at rates approaching those of hydrogenase enzymes.
139                              The immobilized hydrogenase exhibits activity on Si attributable to a bi
140                                              Hydrogenase expression and activity increases in carbon-
141                                              Hydrogenases, ferredoxins, and ferredoxin-NADP(+) reduct
142 llent integration of both photosystem II and hydrogenase for performing the anodic and cathodic half-
143 ecause they may negatively impact the use of hydrogenase for the photoproduction of H2.
144 nickel-containing enzymes, urease and [NiFe]-hydrogenase, for efficient colonization of the human gas
145 ases and ferredoxins from Acetobacterium and hydrogenases, formate dehydrogenase, and cytochromes of
146 c methanogenesis: a coenzyme F(420)-reducing hydrogenase (FrcA) and an iron sulfur protein (MvrD).
147 36 A resolution of the 1.2 MDa F420-reducing hydrogenase (Frh) from methanogenic archaea from only 32
148  screened 48 amino acid substitutions of the hydrogenase from A. macleodii "deep ecotype", to underst
149                                    Using the hydrogenase from Alteromonas macleodii "deep ecotype" as
150  FTIR spectro-electrochemistry on the [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1) at
151 t FTIR electrochemical studies of the [FeFe] hydrogenase from Chlamydomonas reinhardtii, CrHydA1, mat
152 f a hydride-bound state (Hhyd) of the [FeFe]-hydrogenase from Chlamydomonas reinhardtii.
153                                    An [FeFe]-hydrogenase from Clostridium pasteurianum, CpI, is a mod
154                                   The [FeFe] hydrogenase from Desulfovibrio desulfuricans is exceptio
155                     The heterodimeric [NiFe] hydrogenase from Desulfovibrio fructosovorans catalyzes
156  2 N(Gly) 2 )2 ](2+) complex with the [NiFe]-hydrogenase from Desulfovibrio vulgaris immobilized on a
157 by comparing the data obtained with the FeFe hydrogenases from Chlamydomonas reinhardtii and Clostrid
158       We show that the two most studied FeFe hydrogenases, from Chlamydomonas reinhardtii and Clostri
159                The results show promise as a hydrogenase functional mimic derived from a biomolecule.
160 uration (100 s), thus indicating that [FeFe]-hydrogenase functions as an immediate sink for surplus e
161  and YSL16) upregulate the expression of the hydrogenase gene (HYDA) and simultaneously produce hydro
162                                          Two hydrogenase genes, hydA1 and hydA2, were more highly exp
163              The six-iron cofactor of [FeFe]-hydrogenases (H-cluster) is the most efficient H2-formin
164                                      In FeFe hydrogenases, H2 oxidation occurs at the H-cluster, and
165  cofactors and hydride substrate into [NiFe]-hydrogenase (H2ase) active site models.
166 riven H2 production in water with a [NiFeSe]-hydrogenase (H2ase) and a bioinspired synthetic nickel c
167 tron transfer rates increase with increasing hydrogenase (H2ase) enzyme activity.
168  hydrogenation of fumarate to succinate or a hydrogenase (H2ase) for reduction of protons to H2.
169                                   The [NiFe] hydrogenase (H2ase) has been characterized in the Ni-R s
170   No strong phenotype of mutants lacking the hydrogenase has been found.
171                        In contrast, a second hydrogenase has more abundant transcripts in background
172                           The active site of hydrogenases has been a source of inspiration for the de
173 espiratory chains and to subunits of several hydrogenases has raised interest in the evolutionary pat
174          While many synthetic models of [Fe]-hydrogenase have been prepared, none yet are capable of
175 f hydrogen oxidation and evolution by [FeFe]-hydrogenases have been investigated by electrochemical i
176        Certain bacterial enzymes, the diiron hydrogenases, have turnover numbers for hydrogen product
177                                         [Fe] hydrogenase (Hmd) catalyzes the heterolytic splitting of
178 ase activity but had increased bidirectional hydrogenase (Hox) activity.
179 ous cyanobacterium that expresses the uptake hydrogenase HupSL in heterocysts under nitrogen-fixing c
180 w that DosR tightly regulates the two [NiFe]-hydrogenases: Hyd3 (MSMEG_3931-3928) and Hyd2 (MSMEG_271
181 tobutylicum 2[4Fe-4S]-ferredoxin and [Fe-Fe]-hydrogenase HYDA.
182                                   The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has bee
183 s then used for the maturation of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii, to yie
184 the CO/CN(-) stretching vibrations in [FeFe]-hydrogenase HYDA1 from Chlamydomonas reinhardtii.
185  degradation, the highly O2-sensitive [FeFe]-hydrogenase HydA1 from the green algae Chlamydomonas rei
186      H(2) is generated mostly by the [Fe-Fe]-hydrogenase HYDA1, which uses plant type ferredoxin PETF
187 ained, besides a ferredoxin-dependent [FeFe]-hydrogenase (HydA2), a ferredoxin- and NAD-dependent ele
188 nd NAD-dependent electron-bifurcating [FeFe]-hydrogenase (HydABC) that couples the endergonic formati
189 complexes formate dehydrogenase (FdhABC) and hydrogenase (HydABCD) as well as the transcription of th
190           Cyanide reacts rapidly with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Esche
191  an oxygen-tolerant, group 3, soluble [NiFe]-hydrogenase: hydrogenase I from Pyrococcus furiosus (PfS
192 ystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-driven control of elec
193 mplexes of CdS nanorods (CdS NRs) and [FeFe]-hydrogenase I from Clostridium acetobutylicum (CaI).
194 lerant, group 3, soluble [NiFe]-hydrogenase: hydrogenase I from Pyrococcus furiosus (PfSHI), which gr
195 utative proton donor E17 to Q in the soluble hydrogenase I from Pyrococcus furiosus using site direct
196 ccessory proteins from bacteria-synthesizing hydrogenase in the presence of oxygen include HupK, a sc
197 strongly support that the bidirectional NiFe-hydrogenases in cyanobacteria function as electron sinks
198 tonia eutropha, which produces active [NiFe]-hydrogenases in the presence of O2, employs the auxiliar
199                          Here, we show which hydrogenases in Thermococcus paralvinellae are affected
200 igate the progression of O2-dependent [FeFe]-hydrogenase inactivation and the process of H cluster de
201                                              Hydrogenase inactivation is measured during H2 productio
202 ot interfere with measurement of first order hydrogenase inactivation, providing rate constants insen
203 Recent studies on O2-tolerant membrane-bound hydrogenases indicate that the mechanism of O2 tolerance
204  Methanospirillum hungatei were inhibited by hydrogenase inhibitors (cyanide and carbon monoxide), bu
205                                              Hydrogenases interconvert H2 and protons at high rates a
206 pressures, HydS could be a H2-sensing [FeFe]-hydrogenase involved in the regulation of their biosynth
207  of synthetic model complexes of the [Fe-Fe] hydrogenase is investigated, and a dominant role of the
208          Until recently, it was thought that hydrogenase is not active in air-grown microalgal cells.
209        An oxygen-tolerant respiratory [NiFe]-hydrogenase is proven to be a four-electron hydrogen/oxy
210 allic H-cluster at the active site of [FeFe]-hydrogenases is synthesized by three accessory proteins,
211       The light-induced Ni-L state of [NiFe] hydrogenases is well suited to investigate the identity
212 e inhibitor of hydrogen production by [FeFe]-hydrogenases, is used to identify the point in the catal
213 monas reinhardtii is catalyzed by two [FeFe]-hydrogenase isoforms, HydA1 and HydA2, both irreversibly
214 bly of the complex 6Fe active site of [FeFe]-hydrogenases (known as the H-cluster) from its precursor
215 n with a moderate sequence similarity to the hydrogenase large subunit and proposed to participate as
216 way, including two homologs of fdhF encoding hydrogenase-linked formate dehydrogenases (FDHH ) and al
217                                    Using the hydrogenase maturase HydE from Thermotoga maritima as a
218 lternative pathways in a double mutant pgrl1 hydrogenase maturation factor G-2 is detrimental for pho
219 onse to reactive oxygen species, and FDX5 in hydrogenase maturation.
220       Soil organisms harboring high-affinity hydrogenases may be especially competitive, given that t
221                    The membrane-bound [NiFe] hydrogenase (MBH) supports growth of Ralstonia eutropha
222 ing energy from a respiratory membrane-bound hydrogenase (MBH).
223 in the O2-tolerance of membrane-bound [NiFe]-hydrogenase (MBH).
224 oluble subcomplexes of membrane-bound [NiFe]-hydrogenases (MBH) have been extensively studied for app
225 membrane-associated, oxygen-dependent [NiFe] hydrogenases mediate this process.
226 he adjacent Fe-S centers in this O2-tolerant hydrogenase might also be a contributory factor, impedin
227 ble information for the design of artificial hydrogenase mimics.
228 ld provide important clues for the design of hydrogenase mutants with increased resistance to oxidati
229 his precise, solution phase assay for [FeFe] hydrogenase O2 sensitivity and the insights we provide c
230 doxin directly reduce the bidirectional NiFe-hydrogenase of Synechocystis sp. PCC 6803 in vitro.
231       Herein, we report the integration of a hydrogenase on a TiO2 -coated p-Si photocathode for the
232  state known as Ni-L, observed in other NiFe hydrogenases only under illumination or at cryogenic tem
233  RNA-Seq showed consistent expression of six hydrogenase operons with and without added H2 .
234 ration of the chloroplastic oxygen-sensitive hydrogenases or in Proton-Gradient Regulation-Like1 (PGR
235 e ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine.
236 ages, most of the electrons delivered to the hydrogenase originate from water oxidation by PSII, (ii)
237        Metronidazole inhibits the ferredoxin/hydrogenase pathway of fermentative eukaryotic H2 produc
238 nts, or by the progressive activation of the hydrogenase pathway, which provides an electron transfer
239                               The p-Si|TiO2 |hydrogenase photocathode displays visible-light driven p
240 e of O2, employs the auxiliary protein HypX (hydrogenase pleiotropic maturation X) for CO ligand form
241  sets the stage for optimizing the design of hydrogenase-polymer films, and for expanding this strate
242 ime-dependent distribution of species in the hydrogenase/polymer film, using measured or estimated va
243 erial by expressing and maturing the EcHyd-1 hydrogenase prior to expression of the P22 coat protein,
244 ntrolled hydration of three different [FeFe]-hydrogenase proteins produced 8 Hox and 16 Hox-CO specie
245                                Mediated by a hydrogenase, protons reoxidize the fully reduced flavodo
246 e nor evolution of the gas was detected in a hydrogenase quadruple-mutant strain containing deletions
247 analysis of a series of DFT models of [NiFe]-hydrogenases, ranging from minimal NiFe clusters to very
248 etween ferredoxin-NADP(+) oxidoreductase and hydrogenases, rather than due to the sensitivity of hydr
249                We furthermore found that the hydrogenase receives its electrons via pyruvate:flavodox
250 show that the entire pool of cellular [FeFe]-hydrogenase remains active in air-grown cells due to eff
251 bly of the active site [FeFe] unit of [FeFe]-hydrogenases require at least three maturases.
252 ward the discovery of the O2-tolerant [FeFe] hydrogenases required for photosynthetic, biological H2
253                                 Alignment of hydrogenase sequences from sequence databases revealed m
254 ne positions found in a broad survey of NiFe hydrogenase sequences.
255 ydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacter
256           The soluble NAD(+)-reducing [NiFe] hydrogenase (SH) from Ralstonia eutropha couples the rev
257 acity of the soluble, NAD(+)-reducing [NiFe]-hydrogenase (SH) from Ralstonia eutropha H16.
258 oxygen, and we propose that this new type of hydrogenase should be referred to as oxygen-resilient.
259 mally ligating the three FeS clusters in the hydrogenase small subunit.
260 ecifically with VhuD in the absence of other hydrogenase subunits.
261 um Rhizobium leguminosarum contains a single hydrogenase system that can be expressed under two diffe
262 an accessory protein conserved in all [NiFe] hydrogenase systems and involved in the synthesis and tr
263  Hyd-2 is an unusual heterotetrameric [NiFe]-hydrogenase that lacks a typical cytochrome b membrane a
264                                  A different hydrogenase, the hydrogen-evolving Hyc enzyme, removes e
265 aches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H2.
266   Some of us have recently demonstrated that hydrogenases, the fragile but very efficient biological
267                                    In [FeFe]-hydrogenases, the H-cluster cofactor includes a diiron s
268                    The active site of [FeFe] hydrogenases, the H-cluster, consists of a [4Fe-4S] clus
269          Despite extensive studies on [NiFe]-hydrogenases, the mechanism by which these enzymes produ
270 f H2 activation has been proposed for [FeFe]-hydrogenases, the structural and biophysical properties
271 s from approximately 5.8 for the Hox form of hydrogenase to <2 for the CO-inhibited form.
272 ode with a bioanode that utilizes the enzyme hydrogenase to oxidize molecular hydrogen (H2 ) results
273                        The assignment of 156 hydrogenases to 90 different organisms suggests that H2
274 te that it has a unique ability among [NiFe] hydrogenases to catalyze production of H2 even at high p
275 For example, bacteria and archaea use [NiFe]-hydrogenases to catalyze the uptake and release of molec
276                                              Hydrogenases use complex metal cofactors to catalyze the
277 nthetic approach by which to model mono-iron hydrogenase using an anthracene framework, which support
278  unprecedented functional model for the [Fe] hydrogenase, using a Lewis acidic imidazolinium salt as
279 se (FNR) to transfer electrons from NADPH to hydrogenase via ferredoxins (Fd).
280                   Under these conditions the hydrogenase was found to be essential.
281                                    Mono-iron hydrogenase was the third type of hydrogenase discovered
282 far, biosynthesis of the CO ligand in [NiFe]-hydrogenases was unknown.
283 hemical measurements of the turnover rate of hydrogenase, we could resolve the first steps of the inh
284 cycling by a soluble NAD(+) -reducing [NiFe] hydrogenase, we herein present the first bioinspired het
285  effects of FeS cluster attachment in [NiFe] hydrogenase, we undertook a study to substitute all 12 a
286 omly mutated Clostridium pasteurianum [FeFe] hydrogenases, we found a mutant with nearly 3-fold highe
287 ding for ATP synthase, biosynthesis, and Hym hydrogenase were down-regulated during C2H2 inhibition,
288 f a so far unknown type of NAD(P)H-accepting hydrogenase, which is expressed in the presence, but not
289  functional mimic of the active site of [Fe]-hydrogenase, which was developed based on a mechanistic
290                                              Hydrogenases, which catalyze the reversible reduction of
291 s populations appears to be linked with NiFe hydrogenases, which combined with high levels of H2 in m
292 roperties of oxygen-tolerant, group 1 [NiFe]-hydrogenases, which form a single state upon reaction wi
293 etabolism of many anaerobes relies on [NiFe]-hydrogenases, whose characterization when bound to subst
294 gene, which is predicted to encode an [FeFe]-hydrogenase with a C-terminal PAS domain.
295 ic characterization of a CO-inhibited [FeFe] hydrogenase with a selectively (57)Fe-labeled binuclear
296 reaction of Chlamydomonas reinhardtii [FeFe]-hydrogenase with formaldehyde using pulsed-EPR technique
297 istic understanding of catalysis in a [NiFe] hydrogenase with implications in enzymatic proton-couple
298 ive electron flow from photosystem II to the hydrogenase with the production of H2 and O2 being in th
299            The mechanism of reaction of FeFe hydrogenases with oxygen has been debated.
300 the H2 production phase, indicating that the hydrogenase withdraws electrons from the plastoquinone p

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