ライフサイエンスコーパス: hydrogenase

1 g the assembly line toward functional [NiFe]-hydrogenase.

2 O, thereby providing the carbonyl ligand for hydrogenase.

3 of nickel-containing enzymes such as [NiFe]-hydrogenase.

4 f glycine ends up in the CO ligand of [NiFe]-hydrogenase.

5 ding an actinobacteria-type H2-uptake [NiFe]-hydrogenase.

6 , photosystem II, to the H2 evolving enzyme, hydrogenase.

7 of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase.

8 te the proton reduction activity of a [NiFe] hydrogenase.

9 HypC residues relevant for the maturation of hydrogenase.

10 component of the catalytic H-cluster of FeFe hydrogenase.

11 highly fragile catalysts such as the enzyme hydrogenase.

12 of H-cluster maturation occurring within apo-hydrogenase.

13 d all-Fe variants, and the [FeFe] and [NiFe] hydrogenases.

14 ession but decreased expression of all other hydrogenases.

15 the well-studied dinuclear [FeFe] and [NiFe] hydrogenases.

16 ion emulate components of the active site of hydrogenases.

17 it elusive, catalytic intermediate of [NiFe]-hydrogenases.

18 duction of the encapsulated oxygen-sensitive hydrogenases.

19 , FDX9, is potentially the electron donor to hydrogenases.

20 h nickel diphosphine molecular catalysts and hydrogenases.

21 e structure-activity relationships of [FeFe]-hydrogenases.

22 tate bidirectional proton transfer in [FeFe]-hydrogenases.

23 entified in several native and mutant [FeFe]-hydrogenases.

24 erstanding the catalytic mechanism of [FeFe] hydrogenases.

25 E. coli hydrogenase 1 (Hyd-1) is adsorbed on a high surface-area

26 Hydrogenase-1 (Hyd-1) from E. coli poses a conundrum reg

27 es, that the Ni-C to Ni-L interconversion in Hydrogenase-1 (Hyd-1) from Escherichia coli is a pH-depe

28 ide reacts rapidly with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Escherichia coli) u

29 electron entry/exit site in Escherichia coli hydrogenase-1 is shown to play a vital role in tuning bi

30 with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Escherichia coli) under mild oxidizin

31 y that allows synthesizing functional [NiFe]-hydrogenase-2 of Escherichia coli from purified componen

32 comprise a rare example of an active [NiFe]-hydrogenase-4 (Hyd-4) isoenzyme, itself linked to an unu

33 he biosynthesis of the active site of [NiFe]-hydrogenases, a family of H2-activating enzymes.

34 tion-based metabolism featuring a variety of hydrogenases, a streamlined nitrogenase, and electron bi

35 t the organometallic component of the [FeFe]-hydrogenase active site (the H-cluster).

36 anting Mu(.) into three models of the [FeFe]-hydrogenase active site we have been able to detect key

37 g in electrocatalysts inspired by the [NiFe]-hydrogenase active site.

38 This reflects either that H/D exchange at hydrogenase active sites is rapid compared to the rate o

39 As nominal models of hydrogenase active sites, these bimetallics feature two

40 itious O(2) are guided by nature's design of hydrogenase active sites.

41 This highlights the role of hydrogenase activity and PSI-CEF in the ecological succe

42 locality in the chloroplast preserves [FeFe]-hydrogenase activity and supports continuous hydrogen pr

43 Current methods for measuring hydrogenase activity have low throughput and often requi

44 xamined one E. coli strain with undetectable hydrogenase activity in more detail (DeltaeutK), finding

45 This second assay measures the remaining hydrogenase activity in periodic samples taken from the

46 At light onset, hydrogenase activity sustains a linear electron flow fro

47 nases, rather than due to the sensitivity of hydrogenase activity to oxygen.

48 te network of systems that underwrite [NiFe]-hydrogenase activity, including nickel homeostasis and f

49 spite the importance of nickel transport for hydrogenase activity, the sole contribution of yntA and

50 several new genetic components that modulate hydrogenase activity.

51 Aldehyde hydrogenases (ALDHs) belong to a large gene family invol

52 a a periplasmic formate dehydrogenase and/or hydrogenase, allowing energetic coupling to hydrogenotro

53 and expresses the genes for a high-affinity hydrogenase and carbon monoxide dehydrogenase, suggestin

54 H2 PAD-enabled discovery of hydrogenase and FNR mutants that enhance biological H2 p

55 of S. aciditrophicus and S. wolfei had both hydrogenase and formate dehydrogenase activities.

56 Both organisms contain multiple hydrogenase and formate dehydrogenase genes, but lack ge

57 ity of two Ni-containing enzymes, Salmonella hydrogenase and Klebsiella urease.

58 enes involved in the SurR regulon, including hydrogenase and related S(0) -responsive genes.

59 rms a transient interaction complex with the hydrogenase and that the formation of this complex depen

60 embly of the binuclear active site of [NiFe] hydrogenase and the nitrogenase active site cluster FeMo

61 Transcripts of soluble hydrogenases and ferredoxins from Acetobacterium and hyd

62 I possesses electron transfer flavoproteins, hydrogenases and formate dehydrogenases essential for sy

63 hat incorporates catalytically active [FeFe]-hydrogenases and functional partners within the empty sh

64 is may facilitate the design of O(2) -stable hydrogenases and molecular catalysts.

65 Enzymes such as the hydrogenases and nitrogenases are also proposed to invol

66 ntext of the function of the active sites of hydrogenases and nitrogenases.

67 for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.

68 future research efforts in both the study of hydrogenases and the design of molecular catalysts.

69 ones, aldehydes, imines, and carbon dioxide, hydrogenases and their model complexes, and palladium ca

70 of hydride complexes found in nature (e.g., hydrogenases) and in industry (e.g., catalysis and hydro

71 Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform cataly

72 relevance for the catalytic cycle of [FeFe] hydrogenase, and novel strategies for exploring these as

73 oCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and biofuel deve

74 Some Saganbacteria genomes encode various hydrogenases, and others may be able to use O(2) under c

75 ne gene families involved in photosynthesis, hydrogenases, and proteins involved in defense from envi

76 oxygen tolerance in soluble, group 3 [NiFe]-hydrogenases, and we present a model integrating both el

77 [NiFe] hydrogenases are complex model enzymes for the reversibl

78 n this Perspective, hydride states of [FeFe]-hydrogenases are considered on the basis of hydricity, a

79 onic properties of the active site of [NiFe]-hydrogenases are crucial for efficient H2 binding and cl

80 prings reveals that genes encoding oxidative hydrogenases are enriched in communities inhabiting spri

81 [FeFe] hydrogenases are enzymes capable of producing and oxidiz

82 The [FeFe] hydrogenases are generally biased toward proton reductio

83 [FeFe] hydrogenases are highly efficient catalysts for reversib

84 Hydrogenases are metalloenzymes that catalyze the conver

85 [NiFe] hydrogenases are metalloenzymes that catalyze the revers

86 Hydrogenases are metalloenzymes that catalyze the revers

87 Consequently, all hydrogenases are metalloenzymes that contain at least on

88 Oxygen-tolerant [NiFe] hydrogenases are metalloenzymes that represent valuable

89 Hydrogenases are nature's key catalysts involved in both

90 [NiFe]-hydrogenases are redox enzymes composed of a large subun

91 [FeFe] hydrogenases are the best known naturally occurring meta

92 [FeFe] hydrogenases are the most active H(2) converting catalys

93 FeFe hydrogenases are the most efficient H2-producing enzymes

94 ctron and proton transfer pathways in [FeFe]-hydrogenases are well separated from each other in space

95 active sites of a number of enzymes (such as hydrogenases), are promising therapeutic agents, and hav

96 k, we developed a whole-cell high-throughput hydrogenase assay based on the colorimetric reduction of

97 netic optimization of an artificial transfer hydrogenase (ATHase hereafter), [(eta(5)-Cp*)Ir(pico)Cl]

98 lds an NAD(P)H-dependent artificial transfer hydrogenase (ATHase).

99 or a fully renewable H(2) technology, [FeFe]-hydrogenases behave as highly reversible electrocatalyst

100 By coupling our alkB biocathode with a hydrogenase bioanode and using H(2) as a clean fuel sour

101 n, thus overcoming the O2 sensitivity of the hydrogenase, but its activity is low.

102 ring and delivering a precatalyst to the apo-hydrogenase, but the details of this process are not wel

103 cs is recognized for many enzymes, including hydrogenases, but is largely neglected in designing synt

104 he absence of S degrees and have up to seven hydrogenases, but their combined physiological roles are

105 ear active site of an oxygen-tolerant [NiFe] hydrogenase by probing the metal-ligand modes of both th

106 tly, it is shown how the hydricity of [FeFe]-hydrogenases can inspire future research efforts in both

107 sid provides stability and protection to the hydrogenase cargo.

108 In FeFe hydrogenases, catalysis occurs at the H cluster, a metal

109 The [FeFe]-hydrogenase catalytic site H cluster is a complex iron s

110 FeFe hydrogenases catalyze H2 oxidation and formation at an i

111 [FeFe] hydrogenases catalyze proton reduction and hydrogen oxid

112 [FeFe] hydrogenases catalyze rapid H2 production but are highly

113 Hydrogenases catalyze the redox interconversion of proto

114 [NiFe] hydrogenases catalyze the reversible oxidation of molecu

115 The [FeFe]-hydrogenases catalyze the uptake and evolution of hydrog

116 [Fe]-Hydrogenase catalyzes the hydrogenation of a biological

117 ins, is responsible for the synthesis of the hydrogenase CO and CN(-) ligands from tyrosine-derived d

118 gands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligand

119 complex is shown to comprise HycE (a [NiFe] hydrogenase component termed Hyd-3), FdhF (the molybdenu

120 viding rate constants insensitive to initial hydrogenase concentration.

121 The catalytic H-cluster of [FeFe]-hydrogenase consists of a [4Fe-4S] subcluster ([4Fe-4S]H

122 The H-cluster of [FeFe]-hydrogenase consists of a [4Fe-4S](H)-subcluster linked

123 [FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster

124 These results may apply to all [FeFe] hydrogenases containing accessory clusters.

125 tral carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cya

126 The active site of [FeFe] hydrogenase contains a catalytic binuclear iron subsite

127 Hydrogenases couple electrochemical potential to the rev

128 this end, we exposed crystals of the [FeFe]-hydrogenase CpI from Clostridium pasteurianum to oxygen

129 s by site-directed mutagenesis in the [FeFe]-hydrogenase CpI of Clostridium pasteurianum to reveal th

130 ing the Clostridium pasteurianum (Cp) [FeFe] hydrogenase, CpI, we detected significant rates of direc

131 Experiments were carried out on two [FeFe]-hydrogenases, CrHydA1 from the green alga Chlamydomonas

132 ata from an ancient relative, membrane-bound hydrogenase, cryo-EM on mammalian complex I has provided

133 Mycobacterium smegmatis has two such [NiFe] hydrogenases, designated Huc and Hhy, that belong to dif

134 Mono-iron hydrogenase was the third type of hydrogenase discovered.

135 Hydrogenases display a wide range of catalytic rates and

136 Attached to an electrode, hydrogenases display reversible electrocatalytic behavio

137 urthermore, PfSHI, like other group 3 [NiFe]-hydrogenases, does not possess the proximal [4Fe3S] clus

138 is demonstrated for the characterization of hydrogenase during catalytic turnover.

139 We further reveal that group 2a [NiFe] hydrogenases (e.g., Hyd1) can contribute to this process

140 tase (Rnf complex) and the energy-converting hydrogenase (Ech complex).

141 have an energy-converting, ion-translocating hydrogenase (Ech) as a potential respiratory enzyme.

142 microelectrodes were modified with a [NiFe]-hydrogenase embedded in a viologen-modified redox hydrog

143 encoded by dvu0531-dvu0536) and the Fe-only hydrogenase (encoded by dvu1769, hydA and dvu1770, hydB)

144 ional model of the active site of the [FeFe] hydrogenase enzyme.

145 Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors

146 how the H-H bond is oxidized or generated in hydrogenase enzymes.

147 The immobilized hydrogenase exhibits activity on Si attributable to a bi

148 Hydrogenases, ferredoxins, and ferredoxin-NADP(+) reduct

149 llent integration of both photosystem II and hydrogenase for performing the anodic and cathodic half-

150 ecause they may negatively impact the use of hydrogenase for the photoproduction of H2.

151 nickel-containing enzymes, urease and [NiFe]-hydrogenase, for efficient colonization of the human gas

152 ases and ferredoxins from Acetobacterium and hydrogenases, formate dehydrogenase, and cytochromes of

153 FTIR spectro-electrochemistry on the [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1) at

154 y of these intermediate states in the [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1), us

155 ic resonance spectroscopy to an [FeFe] model hydrogenase from Chlamydomonas reinhardtii (CrHydA1), we

156 frared difference spectroscopy on the [FeFe]-hydrogenase from Chlamydomonas reinhardtii evaluating dy

157 t FTIR electrochemical studies of the [FeFe] hydrogenase from Chlamydomonas reinhardtii, CrHydA1, mat

158 f a hydride-bound state (Hhyd) of the [FeFe]-hydrogenase from Chlamydomonas reinhardtii.

159 Recently, an [FeFe] hydrogenase from Clostridium beijerinckii (CbHydA1) was

160 An [FeFe]-hydrogenase from Clostridium pasteurianum, CpI, is a mod

161 The [FeFe] hydrogenase from Desulfovibrio desulfuricans is exceptio

162 The heterodimeric [NiFe] hydrogenase from Desulfovibrio fructosovorans catalyzes

163 2 N(Gly) 2 )2 ](2+) complex with the [NiFe]-hydrogenase from Desulfovibrio vulgaris immobilized on a

164 Using an F(420) -reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzym

165 rdinating [4Fe-4S](H) (Cys362) in the [FeFe] hydrogenase from the green algae Chlamydomonas reinhardt

166 Using the [FeFe]-hydrogenases from Clostridium pasteurianum (CpI) and Chl

167 The [FeFe] hydrogenases from sulfate reducing bacteria can be purif

168 We show that the two most studied FeFe hydrogenases, from Chlamydomonas reinhardtii and Clostri

169 The results show promise as a hydrogenase functional mimic derived from a biomolecule.

170 uration (100 s), thus indicating that [FeFe]-hydrogenase functions as an immediate sink for surplus e

171 Two hydrogenase genes, hydA1 and hydA2, were more highly exp

172 In panel a, the labels 'F420-reducing NiFe hydrogenase (group 3a)' and 'Group 2 NiFe hydrogenase' w

173 lex links a formate dehydrogenase (FDH) to a hydrogenase (H(2)ase) and produces H(2) and CO(2) from f

174 sustain due to 1) competition between [FeFe]-hydrogenase (H(2)ase), the key enzyme responsible for H(

175 The six-iron cofactor of [FeFe]-hydrogenases (H-cluster) is the most efficient H2-formin

176 In FeFe hydrogenases, H2 oxidation occurs at the H-cluster, and

177 tron transfer rates increase with increasing hydrogenase (H2ase) enzyme activity.

178 hydrogenation of fumarate to succinate or a hydrogenase (H2ase) for reduction of protons to H2.

179 The [NiFe] hydrogenase (H2ase) has been characterized in the Ni-R s

180 The active site of hydrogenases has been a source of inspiration for the de

181 While many synthetic models of [Fe]-hydrogenase have been prepared, none yet are capable of

182 [NiFe]-hydrogenases have attracted attention as potential thera

183 [FeFe] hydrogenases have attracted extensive attention in the f

184 f hydrogen oxidation and evolution by [FeFe]-hydrogenases have been investigated by electrochemical i

185 search on the active site cofactor of [FeFe]-hydrogenases have put forward multiple models of the cat

186 [Fe] hydrogenase (Hmd) catalyzes the heterolytic splitting of

187 w that DosR tightly regulates the two [NiFe]-hydrogenases: Hyd3 (MSMEG_3931-3928) and Hyd2 (MSMEG_271

188 The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has bee

189 s then used for the maturation of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii, to yie

190 the CO/CN(-) stretching vibrations in [FeFe]-hydrogenase HYDA1 from Chlamydomonas reinhardtii.

191 degradation, the highly O2-sensitive [FeFe]-hydrogenase HydA1 from the green algae Chlamydomonas rei

192 The enzyme [FeFe]-hydrogenase (HydA1) contains a unique 6-iron cofactor, t

193 ained, besides a ferredoxin-dependent [FeFe]-hydrogenase (HydA2), a ferredoxin- and NAD-dependent ele

194 nd NAD-dependent electron-bifurcating [FeFe]-hydrogenase (HydABC) that couples the endergonic formati

195 complexes formate dehydrogenase (FdhABC) and hydrogenase (HydABCD) as well as the transcription of th

196 Cyanide reacts rapidly with [NiFe]-hydrogenases (hydrogenase-1 and hydrogenase-2 from Esche

197 an oxygen-tolerant, group 3, soluble [NiFe]-hydrogenase: hydrogenase I from Pyrococcus furiosus (PfS

198 ystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-driven control of elec

199 lerant, group 3, soluble [NiFe]-hydrogenase: hydrogenase I from Pyrococcus furiosus (PfSHI), which gr

200 utative proton donor E17 to Q in the soluble hydrogenase I from Pyrococcus furiosus using site direct

201 data demonstrate that the energy-converting hydrogenase in concert with an ATP synthase may be the s

202 ble fashion and is capable of activating apo-hydrogenase in in vitro assays.

203 tonia eutropha, which produces active [NiFe]-hydrogenases in the presence of O2, employs the auxiliar

204 Here, we show which hydrogenases in Thermococcus paralvinellae are affected

205 igate the progression of O2-dependent [FeFe]-hydrogenase inactivation and the process of H cluster de

206 Hydrogenase inactivation is measured during H2 productio

207 ot interfere with measurement of first order hydrogenase inactivation, providing rate constants insen

208 [FeFe] hydrogenases interconvert H(2) into protons and electron

209 Hydrogenases interconvert H2 and protons at high rates a

210 of the hydride ligand proposed for the Ni-C hydrogenase intermediate (Ni(III)-H-Fe(II)).

211 pressures, HydS could be a H2-sensing [FeFe]-hydrogenase involved in the regulation of their biosynth

212 The hydricity of [FeFe]-hydrogenase is also compared to select transition metal

213 Until recently, it was thought that hydrogenase is not active in air-grown microalgal cells.

214 The active site (H-cluster) of [FeFe]-hydrogenases is a blueprint for the design of a biologic

215 allic H-cluster at the active site of [FeFe]-hydrogenases is synthesized by three accessory proteins,

216 e inhibitor of hydrogen production by [FeFe]-hydrogenases, is used to identify the point in the catal

217 monas reinhardtii is catalyzed by two [FeFe]-hydrogenase isoforms, HydA1 and HydA2, both irreversibly

218 bly of the complex 6Fe active site of [FeFe]-hydrogenases (known as the H-cluster) from its precursor

219 way, including two homologs of fdhF encoding hydrogenase-linked formate dehydrogenases (FDHH ) and al

220 uster to bound SAM in the active site of the hydrogenase maturase RS enzyme, HydG, results in specifi

221 lternative pathways in a double mutant pgrl1 hydrogenase maturation factor G-2 is detrimental for pho

222 The membrane-bound [NiFe] hydrogenase (MBH) supports growth of Ralstonia eutropha

223 tem now represented by hydrogen gas-evolving hydrogenase (MBH) where protons are the terminal electro

224 membrane-associated, oxygen-dependent [NiFe] hydrogenases mediate this process.

225 he adjacent Fe-S centers in this O2-tolerant hydrogenase might also be a contributory factor, impedin

226 ble information for the design of artificial hydrogenase mimics.

227 ld provide important clues for the design of hydrogenase mutants with increased resistance to oxidati

228 his precise, solution phase assay for [FeFe] hydrogenase O2 sensitivity and the insights we provide c

229 doxin directly reduce the bidirectional NiFe-hydrogenase of Synechocystis sp. PCC 6803 in vitro.

230 Herein, we report the integration of a hydrogenase on a TiO2 -coated p-Si photocathode for the

231 state known as Ni-L, observed in other NiFe hydrogenases only under illumination or at cryogenic tem

232 RNA-Seq showed consistent expression of six hydrogenase operons with and without added H2 .

233 ration of the chloroplastic oxygen-sensitive hydrogenases or in Proton-Gradient Regulation-Like1 (PGR

234 Metronidazole inhibits the ferredoxin/hydrogenase pathway of fermentative eukaryotic H2 produc

235 nts, or by the progressive activation of the hydrogenase pathway, which provides an electron transfer

236 The p-Si|TiO2 |hydrogenase photocathode displays visible-light driven p

237 e of O2, employs the auxiliary protein HypX (hydrogenase pleiotropic maturation X) for CO ligand form

238 sets the stage for optimizing the design of hydrogenase-polymer films, and for expanding this strate

239 ime-dependent distribution of species in the hydrogenase/polymer film, using measured or estimated va

240 erial by expressing and maturing the EcHyd-1 hydrogenase prior to expression of the P22 coat protein,

241 Each hydrogenase produces 40 molecules of H(2) per second and

242 cover new information about bacterial [NiFe]-hydrogenase production and to probe the cellular compone

243 [NiFe]-hydrogenase production is a complicated process that req

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 actions might affect the hydricity of [FeFe]-hydrogenases, providing a basis for the emulation of the

247 e nor evolution of the gas was detected in a hydrogenase quadruple-mutant strain containing deletions

248 analysis of a series of DFT models of [NiFe]-hydrogenases, ranging from minimal NiFe clusters to very

249 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

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 ydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacter

254 The soluble NAD(+)-reducing [NiFe] hydrogenase (SH) from Ralstonia eutropha couples the rev

255 2)-powered fuel cell with hyper-thermostable hydrogenase (SHI) as the anodic catalyst was combined wi

256 oxygen, and we propose that this new type of hydrogenase should be referred to as oxygen-resilient.

257 [FeFe]-hydrogenases show particularly high rates of hydrogen tu

258 Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H(2))-activat

259 Hyd-2 is an unusual heterotetrameric [NiFe]-hydrogenase that lacks a typical cytochrome b membrane a

260 ostridium pasteurianum produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting

261 H(2)-metabolizing bacteria possess [NiFe] hydrogenases that oxidize H(2) to subatmospheric concent

262 A different hydrogenase, the hydrogen-evolving Hyc enzyme, removes e

263 aches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H2.

264 Some of us have recently demonstrated that hydrogenases, the fragile but very efficient biological

265 In [FeFe]-hydrogenases, the H-cluster cofactor includes a diiron s

266 The active site of [FeFe] hydrogenases, the H-cluster, consists of a [4Fe-4S] clus

267 Despite extensive studies on [NiFe]-hydrogenases, the mechanism by which these enzymes produ

268 ode with a bioanode that utilizes the enzyme hydrogenase to oxidize molecular hydrogen (H2 ) results

269 The assignment of 156 hydrogenases to 90 different organisms suggests that H2

270 For example, bacteria and archaea use [NiFe]-hydrogenases to catalyze the uptake and release of molec

271 ajor roles in the oxidative damage of [FeFe]-hydrogenases under electron-donor deprived conditions pr

272 Hydrogenases use complex metal cofactors to catalyze the

273 nthetic approach by which to model mono-iron hydrogenase using an anthracene framework, which support

274 unprecedented functional model for the [Fe] hydrogenase, using a Lewis acidic imidazolinium salt as

275 of these correlations across a wide range of hydrogenase variants can potentially lead to new insight

276 e driving force and rate of different [FeFe]-hydrogenase variants.

277 se (FNR) to transfer electrons from NADPH to hydrogenase via ferredoxins (Fd).

278 Mono-iron hydrogenase was the third type of hydrogenase discovered

279 far, biosynthesis of the CO ligand in [NiFe]-hydrogenases was unknown.

280 hemical measurements of the turnover rate of hydrogenase, we could resolve the first steps of the inh

281 cycling by a soluble NAD(+) -reducing [NiFe] hydrogenase, we herein present the first bioinspired het

282 omly mutated Clostridium pasteurianum [FeFe] hydrogenases, we found a mutant with nearly 3-fold highe

283 ding for ATP synthase, biosynthesis, and Hym hydrogenase were down-regulated during C2H2 inhibition,

284 Fe hydrogenase (group 3a)' and 'Group 2 NiFe hydrogenase' were misplaced.

285 f a so far unknown type of NAD(P)H-accepting hydrogenase, which is expressed in the presence, but not

286 a focus on the catalytic H-cluster of [FeFe] hydrogenase, which is highly active in producing molecul

287 take of the unique [2Fe(H)] cluster into apo-hydrogenase, which is to date not fully understood.

288 functional mimic of the active site of [Fe]-hydrogenase, which was developed based on a mechanistic

289 moieties that form the catalytic centers of hydrogenases, which are thought to be among the earliest

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 Why does M. smegmatis require two hydrogenases with a seemingly similar function?

300 The mechanism of reaction of FeFe hydrogenases with oxygen has been debated.