ライフサイエンスコーパス: nitrogenase

1 eins (e.g. plant leghemoglobin and bacterial nitrogenase).

2 xing N2 to grow) while containing functional nitrogenase.

3 xygen-dependent conformational protection of nitrogenase.

4 eduction to CH4 in vivo using this remodeled nitrogenase.

5 e biosynthesis of M-cluster, the cofactor of nitrogenase.

6 mental support to hydride-based pathways for nitrogenase.

7 which is later used to synthesize functional nitrogenase.

8 cofactor of Azotobacter vinelandii vanadium nitrogenase.

9 to synthesize H2 as the exclusive product of nitrogenase.

10 ghts into a catalytically competent state of nitrogenase.

11 viding electron transport to the alternative nitrogenase.

12 trates" of DPOR in correlation with those of nitrogenase.

13 rocysts using either a Mo-nitrogenase or a V-nitrogenase.

14 ter) serves as the active site of molybdenum nitrogenase.

15 izes the potential importance of the site in nitrogenase.

16 than merely oxidizing the H2 produced by the nitrogenase.

17 ant resulted in decreased activity of the Mo-nitrogenase.

18 poration of carbon into the FeMoco center of nitrogenase.

19 zymes in nature, except bacterial molybdenum nitrogenase.

20 ty of reducing metalloenzymes in addition to nitrogenase.

21 ents a draft mechanism for N(2) reduction by nitrogenase.

22 of HCO(3)(-)) and the electron flux through nitrogenase.

23 num-iron (MoFe) protein (NifDK) component of nitrogenase.

24 protein, the catalytic component of vanadium nitrogenase.

25 g the Mo- as opposed to the less efficient V-nitrogenase.

26 ibution of electrons and energy available to nitrogenase.

27 rm the iron-molybdenum cofactor (FeMo-co) of nitrogenase.

28 onformationally protected ternary complex of nitrogenase.

29 investigations of the mechanistic details of nitrogenase.

30 NifEN and NifDK, the catalytic component of nitrogenase.

31 ar not been used in its most recent form for nitrogenase.

32 e-protein and the catalytic FeMo-cofactor in nitrogenase.

33 icrobial organisms containing enzymes called nitrogenases.

34 ar to the mechanism of ammonia production by nitrogenases.

35 tion of the active sites of hydrogenases and nitrogenases.

36 atter from diazotrophs using molybdenum (Mo)-nitrogenases.

37 essential to the production of high-yielding nitrogenases.

38 re almost completely covariant among Group I nitrogenases.

39 re derived from the homology between the two nitrogenases.

40 ore Fe sites in the active-site cofactors of nitrogenases.

41 from the activity of a molybdenum-dependent nitrogenase, a complex iron-sulfur enzyme found associat

42 he biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme.

43 by co-illumination of PSII is inhibitory to nitrogenase above a threshold pO(2).

44 Protonated states of the nitrogenase active site are mechanistically significant

45 featuring varying degrees of fidelity to the nitrogenase active site are now known, these complexes f

46 Given that the nitrogenase active site uses weak-field sulfide ligands

47 n of a metal-sulphur cluster that provides a nitrogenase active site.

48 trogenase-related nifB and nifH genes and in nitrogenase activities.

49 ddition of glucose or naphthalene stimulated nitrogenase activity in amended sediments, as detected u

50 diments where strain CJ2 was isolated showed nitrogenase activity in response to dosing with naphthal

51 e DeltahupL mutant demonstrated virtually no nitrogenase activity or H2 production when grown under N

52 trate that this protective complex preserves nitrogenase activity upon exposure to air.

53 Nitrogenase activity was low in the mutant, whereas exog

54 N2 diffused readily into needles and nitrogenase activity was positive across sampling dates.

55 ed the acetylene reduction assay to test for nitrogenase activity within P. flexilis twigs four times

56 that received no carbon addition (showing no nitrogenase activity), no dual-labelled cells were detec

57 ltitude of protective mechanisms to preserve nitrogenase activity, including a "conformational switch

58 aired growth concomitant with a reduction of nitrogenase activity.

59 nitrate exerts rapid and manifold effects on nitrogenase activity.

60 hich prime the intracellular environment for nitrogenase activity.

61 ransferring ATPases found to reduce the MoFe-nitrogenase and 2-hydroxyacyl-CoA dehydratases.

62 mechanisms of the two metalloclusters in Mo-nitrogenase and giving a brief account of the possible a

63 However, nitrogenase and hydrogenase are generally oxygen sensiti

64 Photo-H(2) is shown to occur via nitrogenase and requires illumination of PSI, whereas pr

65 ps of microorganisms that possess functional nitrogenase and/or bidirectional hydrogenases.

66 it was thought to be an essential element of nitrogenases and because it had been established that we

67 rtant to consider in the design of synthetic nitrogenases and may also have broader significance give

68 e HupLS complex helps remove oxygen from the nitrogenase, and that this is a more important function

69 on the iron-molybdenum cofactor (FeMoco) of nitrogenase, and their role in the reduction of N2 to NH

70 s the only transition metal essential to all nitrogenases, and recent biochemical and spectroscopic d

71 [FeFe]-hydrogenses and molybdenum (Mo)-nitrogenase are evolutionarily unrelated enzymes with un

72 Enzymes such as the hydrogenases and nitrogenases are also proposed to involve these structur

73 Molybdenum and vanadium nitrogenases are capable of converting carbon monoxide i

74 Nitrogenases are the enzymes by which certain microorgan

75 Nitrogenases are the only enzymes known to reduce molecu

76 The molybdenum and vanadium nitrogenases are two homologous enzymes with distinct st

77 The molybdenum (Mo)- and vanadium (V)-nitrogenases are two homologous members of this enzyme f

78 dings suggest a possible role of the ancient nitrogenase as an evolutionary link between the carbon a

79 n problem of biological nitrogen fixation in nitrogenase as an example.

80 xation, most probably using molybdenum-based nitrogenase as opposed to other variants that impart sig

81 mpounds show promise as functional models of nitrogenase as substantial amounts of NH3 are produced u

82 avior of these variants are characterized by nitrogenase assay and strand-specific RNA sequencing (RN

83 Laboratory growth and nitrogenase assays verified that these genes are functio

84 proteins from two phylogenetically distinct nitrogenases (Azotobacter vinelandii, Av, and Clostridiu

85 oa) mechanism for reduction of N2 to 2NH3 by nitrogenase, based on identification of a freeze-trapped

86 rbons suggests the feasibility of developing nitrogenase-based biomimetic approaches to recycle C1 wa

87 ofactors suggests the possibility to develop nitrogenase-based electrocatalysts for the production of

88 leads us to propose that NO2(-) reduction by nitrogenase begins with the generation of NO2H bound to

89 the reduction of CO2 is reported, with the V nitrogenase being capable of reducing CO2 to CO, CD4, C2

90 Nitrogenase biosynthesis protein NifB catalyzes the radi

91 ) is not reduced by the wild-type molybdenum nitrogenase but instead inhibits the reduction of all su

92 , fixes nitrogen via the oxygen-sensitive Mo nitrogenase but is also able to fix nitrogen through the

93 uenced to date encode a molybdenum-dependent nitrogenase, but some also have alternative nitrogenases

94 me of these are able to rapidly "switch-off" nitrogenase, by shifting the enzyme into an inactive but

95 ed by changing the flux of electrons through nitrogenase, by substitution of other amino acids locate

96 We demonstrate in vitro that nitrogenase can be oxidatively damaged under anoxic cond

97 These findings show that alternative nitrogenase can no longer be neglected in natural ecosys

98 re of the central mechanistic steps by which nitrogenase carries out one of the most challenging chem

99 the P(OX) state is functionally relevant in nitrogenase catalysis and that a hard, O-based anionic l

100 though the role of this interstitial atom in nitrogenase catalysis is unknown, progress in understand

101 ween FeP and MoFeP play a functional role in nitrogenase catalysis.

102 s in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure.

103 The exciting observation of a V nitrogenase-catalyzed C-C coupling with CO2 as the origi

104 The enzyme nitrogenase catalyzes H2 formation.

105 Nitrogenase catalyzes substrate reduction at its cofacto

106 The Mo nitrogenase catalyzes the ambient reduction of N2 to NH3

107 Nitrogenase catalyzes the ATP-dependent reduction of din

108 The molybdenum-dependent nitrogenase catalyzes the multi-electron reduction of pr

109 Nitrogenase catalyzes the reduction of dinitrogen (N2) t

110 Nitrogenase catalyzes the reduction of N(2) and protons

111 The two-component metalloprotein nitrogenase catalyzes the reductive fixation of atmosphe

112 The coupling of this nitrogenase cathode with a bioanode that utilizes the en

113 rophores are used for the acquisition of the nitrogenase co-factors Mo and V.

114 The fate of the interstitial atom of the nitrogenase cofactor during substrate turnover has remai

115 stitial carbon atom recently assigned in the nitrogenase cofactor may have a similar role, perhaps by

116 protein other than NifDK to house the unique nitrogenase cofactor.

117 All known nitrogenase cofactors are rich in both sulfur and iron a

118 Nitrogenase cofactors can be extracted into an organic s

119 Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP

120 communication between the two halves of the nitrogenase complex is suggested by normal-mode calculat

121 tructure of the Fe protein in the stabilized nitrogenase complex structures.

122 63% of the ATP-coupled reaction rate for the nitrogenase complex under optimal conditions.

123 he surface properties and known complexes of nitrogenase component proteins allow us to propose a mod

124 chieve this multielectron redox process, the nitrogenase component proteins, MoFe-protein (MoFeP) and

125 he convenience of using mitochondria to host nitrogenase components, thus providing instrumental tech

126 d reduced N2-fixation rates despite elevated nitrogenase concentrations.

127 Mo nitrogenase consists of two component proteins: the Fe p

128 A purified remodeled nitrogenase containing two amino acid substitutions near

129 The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented mu(6)-

130 alysis, that the molybdenum-iron cofactor of nitrogenase contains two [Fe-H(-)-Fe] bridging-hydride f

131 understanding of the mechanistic features of nitrogenase could be relevant to the design of synthetic

132 of genetically distinct alternative forms of nitrogenase designated the Vnf and Anf systems when Mo i

133 ed Fe6(RHH)) into the catalytic component of nitrogenase (designated NifDK(apo)).

134 biosynthetic scaffold for the cofactor of Mo-nitrogenase (designated the M-cluster).

135 s the capacity for nitrogen fixation using a nitrogenase distinct from that in Cyanobacteria, suggest

136 proposed to form at the active site of MoFe-nitrogenase during catalytic dinitrogen reduction to amm

137 Freeze-quenching nitrogenase during turnover with N2 traps an S = (1/2) i

138 This subunit may be relevant to consider in nitrogenases during turnover.

139 The heterocyst-specific nitrogenase encoded by the large nif1 gene cluster and t

140 f either the nitrogen fixing bacteria or the nitrogenase enzyme responsible for nitrogen fixation.

141 lized cells that protect their oxygen-labile nitrogenase enzyme system; (3) the earliest known fossil

142 hermophilic chemolithoautotroph with a novel nitrogenase enzyme that is oxygen-insensitive.

143 BNF is mediated by the nitrogenase enzyme, which, in its most common form, requ

144 itation were inferred based on expression of nitrogenase enzymes and phosphate uptake proteins.

145 iates in biological nitrogen fixation by the nitrogenase enzymes and the industrial Haber-Bosch hydro

146 Nitrogenase enzymes are used by microorganisms for conve

147 appreciated that the iron-rich cofactors of nitrogenase enzymes facilitate this transformation, how

148 Nitrogenase enzymes mediate the six-electron reductive c

149 molecular nitrogen-fixing systems, including nitrogenase enzymes, are of much interest but are not fu

150 the reduction of all substrates catalyzed by nitrogenase except protons.

151 an evolutionary relic of the function of the nitrogenase family.

152 Azotobacter vinelandii nitrogenase Fe protein (Av2) provides a rare opportunity

153 The nitrogenase Fe protein cycle involves a transient associ

154 Recently, a kinetic study of the nitrogenase Fe protein cycle involving the physiological

155 r studies of electron transfer (ET) from the nitrogenase Fe protein to the MoFe protein concluded tha

156 cA was competent for rapid activation of apo-nitrogenase Fe protein under anaerobic conditions.

157 that aerobically grown cells express active nitrogenase Fe protein when the NifH polypeptide is targ

158 nd to donate clusters to the apo form of the nitrogenase Fe-protein.

159 Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase en

160 progress on [FeFe]-hydrogenase H cluster and nitrogenase FeMo-cofactor assembly in the context of the

161 Assembly of nitrogenase FeMoco is one of the key processes in bioino

162 sms of the P-cluster and cofactor species of nitrogenase, focusing on what is known about the assembl

163 Under these conditions the two components of nitrogenase form a stable, ternary complex with a small

164 he M cluster, the cofactor of the molybdenum nitrogenase from Azotobacter vinelandii.

165 y respiratory O2 uptake in the protection of nitrogenase from oxidative damage and, thus, in an effic

166 ementioned conformational switch can protect nitrogenase from such damage, confirming that the confor

167 A central puzzle of nitrogenase function is an apparently obligatory formati

168 Phylogenetic analysis of the UCYN-A nitrogenase gene (nifH) showed that the UCYN-A lineage i

169 d N2fixation at all six stations, studies of nitrogenase gene abundance and expression from the same

170 The nitrogenase gene cluster in cyanobacteria has been thoug

171 ly of proteins are the primary activators of nitrogenase gene expression in cyanobacteria.

172 QD-PEI (10 nM) induced three types of nitrogenase genes (nif, anf, and vnf) in A. vinelandii,

173 H. schlegelii similarly lacks nitrogenase genes and is a non-diazotroph.

174 yngbya species are reported to fix nitrogen, nitrogenase genes were not found in the genome or by PCR

175 The FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon,

176 talyze the reduction of nitrogen to ammonia, nitrogenase has a surprising rapport with carbon-both th

177 -electron/eight-proton catalytic reaction of nitrogenase has been hampered by the fact that electron

178 In the present study, the mechanism for nitrogenase has been investigated by hybrid DFT using a

179 he iron-molybdenum active site of the enzyme nitrogenase has inspired chemists to explore iron and mo

180 n a small-scale reaction, vanadium-dependent nitrogenase has previously been shown to catalyze reduct

181 ifferences and similarities between DPOR and nitrogenase have broad implications for the energy trans

182 all atoms in the iron-molybdenum cofactor of nitrogenase have finally been elucidated, and the discov

183 tomically homologous active site in vanadium nitrogenase, highlights the importance and influence of

184 Inhibitors of nitrogenase (i.e., acetylene, carbon monoxide, and dihyd

185 n contribute to ongoing efforts of mimicking nitrogenase in fixing nitrogen and point to a promising

186 fixing bacteria prolong the functionality of nitrogenase in molybdenum starvation by a special Mo sto

187 provide energetic and kinetic advantages to nitrogenase in the complex mechanism of N(2) reduction.

188 Overexpression of the V-nitrogenase in the double vnfR1 vnfR2 mutant resulted in

189 ed the use of the alternative vanadium-based nitrogenase in the Nostoc cyanobiont of these lichens an

190 tant lacking both VnfR1 and VnfR2 made the V-nitrogenase in the presence of Mo.

191 The differential activities of the V and Mo nitrogenases in CO2 reduction provide an important frame

192 erein, a similar discrepancy between the two nitrogenases in the reduction of CO2 is reported, with t

193 o be essential for nitrogen fixation by FeFe nitrogenase, including nifM, vnfEN, and anfOR, are not r

194 tion of nitrite (NO2(-)) to ammonia (NH3) by nitrogenase indicate a limiting stoichiometry, NO2(-) +

195 A nitrogenase-inspired biomimetic chalcogel system compris

196 (FeSII, or "Shethna") that reversibly locks nitrogenase into a multicomponent protective complex upo

197 e recently demonstrated that N2 reduction by nitrogenase involves the obligatory release of one H2 pe

198 an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster).

199 Nitrogenase is a complex enzyme that catalyzes the reduc

200 Nitrogenase is a versatile metalloenzyme that is capable

201 es with an earlier study to demonstrate that nitrogenase is activated for N2 binding and reduction th

202 Nitrogenase is activated for N2 reduction by the accumul

203 ole for the alternative nitrogenases over Mo-nitrogenase is also consistent with evidence of Mo scarc

204 Nitrogenase is an ATP-requiring enzyme capable of carryi

205 The FeMoco of nitrogenase is an iron-sulfur cluster with exceptional b

206 hat an A. vinelandii strain expressing the V-nitrogenase is capable of in vivo reduction of CO to eth

207 e of the previously proposed oxygen-tolerant nitrogenase is extremely unlikely.

208 The P-cluster of nitrogenase is largely known for its function to mediate

209 ed state (P(OX)) is involved in catalysis by nitrogenase is not well established.

210 Nitrogen activation by nitrogenase is one of the most important enzymatic proce

211 , expression of the three different types of nitrogenase is regulated in response to metal availabili

212 e:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catal

213 Nitrogenase is the only enzyme that can convert atmosphe

214 The active site of the molybdenum-dependent nitrogenase is the unique carbide-containing iron-sulfur

215 component of the iron-molybdenum cofactor of nitrogenase, is essential for symbiotic nitrogen fixatio

216 he iron-molybdenum cofactor (FeMoco) of MoFe-nitrogenase, its role is unknown.

217 protochlorophyllide oxidoreductase (DPOR), a nitrogenase-like metalloenzyme, catalyzes the chemically

218 C7-C8 double bond of chlorophyllide a by the nitrogenase-like multisubunit metalloenzyme, chlorophyll

219 volution is associated with hydrogenases and nitrogenase, making these enzymes interesting targets fo

220 ely distributed protein family that includes nitrogenase maturation factors, NifB and NifX.

221 Furthermore, it is shown that the V nitrogenase may direct the formation of CD4 in part via

222 tions of these findings in understanding the nitrogenase mechanism and the relationship to Fischer-Tr

223 tures of increasingly higher resolution, the nitrogenase mechanism is still not understood.

224 This study not only reveals the nitrogenase mechanism of H2 formation by hydride protona

225 tial carbide and providing insights into the nitrogenase mechanism.

226 Next, a primitive homolog of nitrogenase mediates a six-electron reduction and gamma-

227 e, we report the formation of an artificial, nitrogenase-mimicking enzyme upon insertion of a synthet

228 A doubly substituted form of the nitrogenase MoFe protein (alpha-70(Val)(-->Ala), alpha-1

229 Here, we report that when the nitrogenase MoFe protein alpha-Val(70) residue is substi

230 : X-ray anomalous diffraction studies on the nitrogenase MoFe protein show the presence of a mononucl

231 te iron-molybdenum cofactor (FeMo-co) of the nitrogenase MoFe protein undergoes six steps of hydrogen

232 x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoc

233 inds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-

234 crystallography and EPR spectroscopy of the nitrogenase molybdenum iron (MoFe) proteins from two phy

235 nocrystals can be used to photosensitize the nitrogenase molybdenum-iron (MoFe) protein, where light

236 structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angst

237 l-4,4'-bipyridinium) to shuttle electrons to nitrogenase, N2 reduction to NH3 can be mediated at an e

238 CO-inhibited Azotobacter vinelandii (Av) Mo-nitrogenase (N2ase) have been examined by the combined a

239 The NH3 generated from nitrogenase (N2ase) in X. autotrophicus can be diverted

240 first known halogen-containing substrate by nitrogenase (N2ase), 3,3-difluorocyclopropene (DFCP), wa

241 ge color morphs expressed significantly more nitrogenase (nifH) transcripts consistent with their kno

242 Genes encoding nitrogenase (nifH) were amplified from sediment and phot

243 the Deltaflv3B strain has reduced amounts of nitrogenase NifHDK subunits and shows multiple symptoms

244 pressure, whereas N2 fixation by the enzyme nitrogenase occurs under ambient conditions using chemic

245 The vanadium (V)-nitrogenase of Azotobacter vinelandii catalyses the in v

246 n genes previously published as the putative nitrogenase of S. thermoautotrophicus have little simila

247 d cells called heterocysts using either a Mo-nitrogenase or a V-nitrogenase.

248 A significant role for the alternative nitrogenases over Mo-nitrogenase is also consistent with

249 it is required for the activity of bacterial nitrogenase, plant leghemoglobin, respiratory oxidases,

250 nadium (V)- and iron (Fe)-only "alternative" nitrogenases produce fixed N with significantly lower de

251 lism, so that although the metal clusters of nitrogenase rapidly decompose in the presence of dioxyge

252 The overall nitrogenase rate-limiting step is associated with ATP-dr

253 The most common nitrogenases reduce atmospheric N2 at the FeMo cofactor,

254 Nitrogenase reduces dinitrogen (N2) to ammonia in biolog

255 on was also observed in the transcription of nitrogenase-related nifB and nifH genes and in nitrogena

256 The mechanism of nitrogenase remains enigmatic, with a major unresolved i

257 Fe]-hydrogenases and the FeMo cofactor of Mo-nitrogenase require specific maturation machinery for th

258 ction of N2 to NH3 catalyzed by Mo-dependent nitrogenase requires at least eight rounds of a complex

259 rd in overcoming the crippling limitation of nitrogenase's sensitivity toward O2.

260 l protonation sites at the active site among nitrogenase species.

261 asize the benefits of investigating multiple nitrogenase species.

262 substrate for both molybdenum- and vanadium-nitrogenases strengthens the hypothesis that CO reductio

263 V-nitrogenase structural genes, vnfDGK, as well as vnfEN f

264 tion intermediate hydroxylamine (NH2OH) is a nitrogenase substrate for which the H and I reduction in

265 Its reactions with nitrogenase substrates show that the hydride can act as

266 etic systems, which can bind N2, reduce some nitrogenase substrates, and/or reductively eliminate H2

267 sed genes for nitrite reductase (nirS) and a nitrogenase subunit (nifH) was used to identify the like

268 osed N2 binding step at the FeMo cofactor of nitrogenase, suggesting the use of the present bimetalli

269 etween the CO-reducing capacities of the two nitrogenases suggests that the identity of heterometal a

270 ete complement of genes associated with each nitrogenase system and the extent of cross talk between

271 assis to build an artificial iron-only (Anf) nitrogenase system composed of defined anf and nif genes

272 ng has enabled us to engineer a minimal FeFe nitrogenase system comprising the structural anfHDGK gen

273 n in this strain is mediated by an efficient nitrogenase system, which can be manipulated to convert

274 We recently presented a draft mechanism for nitrogenase that provides an explanation for obligatory

275 nitrogenase, but some also have alternative nitrogenases that are dependent on either vanadium (VFe)

276 yanobacterium Anabaena variabilis has two Mo-nitrogenases that function under different environmental

277 The catalytic center of nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor

278 ctors (molybdenum (Mo) and iron (Fe)) of the nitrogenase, the enzyme responsible for the reduction of

279 The active site of nitrogenase, the M-cluster, is a metal-sulfur cluster co

280 Nitrogenase, the only enzyme known to be able to reduce

281 e "M-cluster" molybdenum prosthetic group of nitrogenase; the biosynthesis of the nickel-based metall

282 ork together with the reductase component of nitrogenase to reduce C2H2 in an ATP-dependent reaction.

283 ons avoids strong reductants, and may enable nitrogenase to reduce multiple bonds without unreasonabl

284 uisition and the contribution of alternative nitrogenases to BNF in the ubiquitous cyanolichen Peltig

285 An important contribution of alternative nitrogenases to N2 fixation provides a simple explanatio

286 The extreme sensitivity of nitrogenase towards oxygen stands as a major barrier to

287 A cnfR1 mutant was unable to make nitrogenase under aerobic conditions in heterocysts whil

288 NifA that is able to activate expression of nitrogenase under all growth conditions.

289 ts while the cnfR2 mutant was unable to make nitrogenase under anaerobic conditions.

290 Rapid freezing of a modified nitrogenase under turnover conditions using diazene, met

291 tes freeze-trapped during NO2(-) turnover by nitrogenase variants and investigated by Q-band ENDOR/ES

292 Previously, it was demonstrated that the V nitrogenase was nearly 700 times more active than its Mo

293 assembly schemes of their counterparts in V-nitrogenase, which are derived from the homology between

294 ure has been motivating people to learn from nitrogenase, which can fix atmospheric N2 to NH3 in vivo

295 The evolution of the nitrogen-fixing enzyme nitrogenase, which reduces atmospheric N2 to organic NH4

296 sed for the activation of carbon monoxide by nitrogenase, which suggests an essential role of the int

297 alustris required constitutive expression of nitrogenase, which was achieved by using a variant of th

298 cent studies have suggested that alternative nitrogenases, which use vanadium or iron in place of mol

299 tems, silica-supported tantalum hydrides and nitrogenase will be discussed.

300 Azotobacter chroococcum expresses iron-rich nitrogenases, with which it reduces N2 .