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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.
22 es, that the Ni-C to Ni-L interconversion in Hydrogenase-1 (Hyd-1) from Escherichia coli is a pH-depe
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
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
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
36 This reflects either that H/D exchange at hydrogenase active sites is rapid compared to the rate o
39 locality in the chloroplast preserves [FeFe]-hydrogenase activity and supports continuous hydrogen pr
41 cellular compartments, including detectable hydrogenase activity in Mastigamoeba cytosol and mitocho
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
56 g postulates a direct link between CrPFO and hydrogenase and provides new opportunities to better stu
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
64 ones, aldehydes, imines, and carbon dioxide, hydrogenases and their model complexes, and palladium ca
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
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
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]
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
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
113 tral carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cya
116 and activation in the active site of [NiFe]-hydrogenases could be exploited in the design of novel b
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
122 ression of HYDA and the specific activity of hydrogenase demonstrate that C. vulgaris YSL01 and YSL16
125 urthermore, PfSHI, like other group 3 [NiFe]-hydrogenases, does not possess the proximal [4Fe3S] clus
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
132 ions, including the oxidation of hydrogen by hydrogenase enzymes and ionic hydrogenation of organic c
135 Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors
142 llent integration of both photosystem II and hydrogenase for performing the anodic and cathodic half-
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
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
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
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
166 riven H2 production in water with a [NiFeSe]-hydrogenase (H2ase) and a bioinspired synthetic nickel c
173 espiratory chains and to subunits of several hydrogenases has raised interest in the evolutionary pat
175 f hydrogen oxidation and evolution by [FeFe]-hydrogenases have been investigated by electrochemical i
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
183 s then used for the maturation of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii, to yie
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
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
200 igate the progression of O2-dependent [FeFe]-hydrogenase inactivation and the process of H cluster de
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
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
210 allic H-cluster at the active site of [FeFe]-hydrogenases is synthesized by three accessory proteins,
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
218 lternative pathways in a double mutant pgrl1 hydrogenase maturation factor G-2 is detrimental for pho
224 oluble subcomplexes of membrane-bound [NiFe]-hydrogenases (MBH) have been extensively studied for app
226 he adjacent Fe-S centers in this O2-tolerant hydrogenase might also be a contributory factor, impedin
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.
232 state known as Ni-L, observed in other NiFe hydrogenases only under illumination or at cryogenic tem
234 ration of the chloroplastic oxygen-sensitive hydrogenases or in Proton-Gradient Regulation-Like1 (PGR
236 ages, most of the electrons delivered to the hydrogenase originate from water oxidation by PSII, (ii)
238 nts, or by the progressive activation of the hydrogenase pathway, which provides an electron transfer
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
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
250 show that the entire pool of cellular [FeFe]-hydrogenase remains active in air-grown cells due to eff
252 ward the discovery of the O2-tolerant [FeFe] hydrogenases required for photosynthetic, biological H2
255 ydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacter
258 oxygen, and we propose that this new type of hydrogenase should be referred to as oxygen-resilient.
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
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
270 f H2 activation has been proposed for [FeFe]-hydrogenases, the structural and biophysical properties
272 ode with a bioanode that utilizes the enzyme hydrogenase to oxidize molecular hydrogen (H2 ) results
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
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
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
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
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
300 the H2 production phase, indicating that the hydrogenase withdraws electrons from the plastoquinone p
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