ライフサイエンスコーパス: nitrogenase

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

2 y in iron-sulfur clusters like the FeMoco of nitrogenase.

3 er reduces hydrazine, a natural substrate of nitrogenase.

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

5 xing N2 to grow) while containing functional nitrogenase.

6 which is later used to synthesize functional nitrogenase.

7 ibution of electrons and energy available to nitrogenase.

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

9 onformationally protected ternary complex of nitrogenase.

10 investigations of the mechanistic details of nitrogenase.

11 NifEN and NifDK, the catalytic component of nitrogenase.

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

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

14 xygen-dependent conformational protection of nitrogenase.

15 eduction to CH4 in vivo using this remodeled nitrogenase.

16 challenge in the heterologous expression of nitrogenase.

17 lance to a pair of E(n) and E(n+2) states of nitrogenase.

18 nues for studying the catalytic mechanism of nitrogenase.

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

20 mental support to hydride-based pathways for nitrogenase.

21 cofactor of Azotobacter vinelandii vanadium nitrogenase.

22 ofactor to NifDK, the catalytic component of nitrogenase.

23 tural and functional similarity between each nitrogenase.

24 found in microbes that also have molybdenum nitrogenase.

25 conformationally gated electron transfer in nitrogenase.

26 the least-studied of which is the iron-only nitrogenase.

27 re almost completely covariant among Group I nitrogenases.

28 re derived from the homology between the two nitrogenases.

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

30 icrobial organisms containing enzymes called nitrogenases.

31 contributions to interpreting the nature of nitrogenases.

32 nvestigations into the reaction mechanism of nitrogenases.

33 nitrogenase, ~4-7 for Fe-nitrogenase) and Mo-nitrogenase (~1) measured here are lower than prior in v

34 s in H(2) :N(2) stoichiometry by alternative nitrogenases (~1.5 for V-nitrogenase, ~4-7 for Fe-nitrog

35 usion barrier that protects oxygen-sensitive nitrogenase [11, 12], and cyanobacteria typically exhibi

36 etry by alternative nitrogenases (~1.5 for V-nitrogenase, ~4-7 for Fe-nitrogenase) and Mo-nitrogenase

37 The size and complexity of Mo-dependent nitrogenase, a multicomponent enzyme capable of reducing

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

39 els, there is a strong need to elucidate how nitrogenase achieves this difficult reaction under benig

40 Protonated states of the nitrogenase active site are mechanistically significant

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

42 ar active site of [NiFe] hydrogenase and the nitrogenase active site cluster FeMoco.

43 oS(2-x) basal plane mimicking the natural Mo-nitrogenase active site is modified by Co doping and exh

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

45 G. magellanica presented some of the highest nitrogenase activities yet reported (potential maximal c

46 ribution and speciation in nodules, reducing nitrogenase activity and biomass production.

47 is upregulated in association with increased nitrogenase activity and causes a monotonic decrease in

48 Nitrogenase activity assays of these resistant variants

49 Here, we engineer inducible nitrogenase activity in two cereal endophytes (Azorhizob

50 sm to accommodate the energy requirement for nitrogenase activity is largely unknown.

51 ium tolerance and higher oxygen tolerance of nitrogenase activity than that from K. oxytoca.

52 R. sp. IRBG74 can be engineered to result in nitrogenase activity under free-living conditions by tra

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

54 Nitrogenase activity was low in the mutant, whereas exog

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

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

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

58 ics in response to ammonium availability and nitrogenase activity.

59 d reducing equivalents required for elevated nitrogenase activity.

60 aired growth concomitant with a reduction of nitrogenase activity.

61 ) production and NADH recycling catalyzed by nitrogenase and diaphorase.

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

63 e pathway for the heterologous expression of nitrogenase and identifying variants for the mechanistic

64 lysis include the Fe-Mo cofactor (FeMoco) of nitrogenase and its V and all-Fe variants, and the [FeFe

65 ed methyl viologen (MV(*+)) and NADH for the nitrogenase and l-alanine dehydrogenase.

66 he potential landscape in the active site of nitrogenase and revealing the endergonic nature of elect

67 dual aims of better understanding biological nitrogenases and improving upon industrial nitrogen fixa

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

69 e-like reductase that is distinct from known nitrogenases and nitrogenase-like reductases and specifi

70 genases (~1.5 for V-nitrogenase, ~4-7 for Fe-nitrogenase) and Mo-nitrogenase (~1) measured here are l

71 ing a variety of hydrogenases, a streamlined nitrogenase, and electron bifurcating complexes involved

72 trogenases that are homologous to molybdenum nitrogenases are also found in archaea and bacteria, but

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

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

75 The presumption has been that alternative nitrogenases are fail-safe enzymes that are used in situ

76 Nitrogenases are responsible for biological nitrogen fix

77 Nitrogenases are the enzymes by which certain microorgan

78 Nitrogenases are the only enzymes known to reduce molecu

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

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

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

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

83 nd mechanistic proposals for the alternative nitrogenases as well as their electronic and structural

84 )-linker-NifK retained function in bacterial nitrogenase assays, demonstrating that this polyprotein

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

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

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

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

89 Nitrogen fixation by nitrogenase begins with the accumulation of four reducin

90 occupies a central and essential position in nitrogenase biogenesis.

91 Nitrogenase biosynthesis protein NifB catalyzes the radi

92 carbide in the FeMo cofactor of Mo-dependent nitrogenase, but has proven to be a synthetic challenge.

93 . nitrogen-fixing) growth with the iron-only nitrogenase, but its enzymatic activity and function are

94 se enzymes were analogously active as the Mo-nitrogenase, but more recent investigations have found c

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

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

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

102 Nitrogenases catalyze the reduction of N(2) to NH(4) (+)

103 Nitrogenase catalyzes substrate reduction at its cofacto

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

105 Nitrogenase catalyzes the ATP-dependent reduction of din

106 summarizes recent progress in addressing how nitrogenase catalyzes the reduction of an array of subst

107 Nitrogenase catalyzes the reduction of dinitrogen (N2) t

108 Molybdenum nitrogenase catalyzes the reduction of dinitrogen into a

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

110 plays a crucial role in the biosynthesis of nitrogenase, catalyzing the final step of cofactor matur

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

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

113 ethionine (SAM) enzyme that is essential for nitrogenase cofactor assembly.

114 or the formation of the key precursor in the nitrogenase cofactor biosynthetic pathway in a eukaryoti

115 ovides a critical overview of discoveries on nitrogenase cofactor structure, function, and activity o

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

117 uired for the assembly of an 8Fe core of the nitrogenase cofactor.

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

119 Nitrogenase cofactors can be extracted into an organic s

120 nsights into the electronic structure of the nitrogenase cofactors.

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

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

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

124 63% of the ATP-coupled reaction rate for the nitrogenase complex under optimal conditions.

125 associated with each metallocofactor of the nitrogenase complex, illuminating the role of nitrogenas

126 chanism observed in the structurally related nitrogenase complex.

127 ediates of CdS quantum dot (QD):MoFe protein nitrogenase complexes under photochemical activation usi

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

129 ctural and thermodynamic redox properties of nitrogenase component proteins and their complexes, as w

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

131 a [4Fe-4S] cluster located at the Fe protein nitrogenase component.

132 requires the participation of the structural nitrogenase components and many accessory proteins, and

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

134 The Mo-dependent nitrogenase comprises two interacting components called

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

136 Molybdenum-dependent nitrogenase consists of two proteins and three metalloco

137 A purified remodeled nitrogenase containing two amino acid substitutions near

138 The enzyme molybdenum nitrogenase converts atmospheric nitrogen gas to ammonia

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

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

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

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

143 decreases under OA primarily due to reduced nitrogenase efficiency.

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

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

146 the biosphere is reduction to ammonia by the nitrogenase enzyme, which is inactivated by oxygen.

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

148 is catalyzed by the extremely O(2)-sensitive nitrogenase enzyme.

149 nt geometric features of N(2) binding by the nitrogenase enzymes and Mittasch catalysts would contrib

150 Nitrogenase enzymes are the only biological catalysts ab

151 Nitrogenase enzymes are used by microorganisms for conve

152 Nitrogenase enzymes catalyze the reduction of atmospheri

153 Nitrogenase enzymes mediate the six-electron reductive c

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

155 The activity of nitrogenase enzymes, which catalyze the conversion of at

156 the role of the secondary sphere residues in nitrogenase enzymes.

157 fix atmospheric nitrogen gas to ammonium via nitrogenase enzymes.

158 and relatedly as intermediates of N(2)RR by nitrogenase enzymes.

159 Three types of nitrogenase exist, the least-studied of which is the iro

160 n to eliminate ammonium repression and place nitrogenase expression under the control of agricultural

161 Disabling native regulation can turn on nitrogenase expression, even in the presence of nitrogen

162 The nitrogenase Fe protein cycle involves a transient associ

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

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

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

166 on environment similar to the active site of nitrogenase (FeMoco) and thus demonstrate reasonable mec

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

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

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

170 We predict that Anf3 protects the iron-only nitrogenase from oxygen inactivation by functioning as a

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

172 in space or time are involved in protecting nitrogenase from the intracellular O(2) evolved by photo

173 To engineer Mo-dependent nitrogenase function in plants, expression of the struct

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

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

176 have found that the 'alternative' V- and Fe-nitrogenases generally reduce N(2) more slowly and produ

177 iales), reflected in increased abundances of nitrogenase genes (nifH), catalyzed biodegradation of th

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

179 sly assumed, helping explain why alternative nitrogenase genes persist in diverse diazotroph lineages

180 Quantitative assessment of Dhc nitrogenase genes, transcripts, and proteomics data link

181 Nitrogenase harbors three distinct metal prosthetic grou

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

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

184 While the kinetics of isolated nitrogenase has been extensively studied, little is know

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

186 So far alternative nitrogenases have only been found in microbes that also

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

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

189 diffusion across their membranes to protect nitrogenase in ambient O(2)-saturated surface ocean wate

190 They are less widespread than molybdenum nitrogenase in bacteria and archaea, and they are less e

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

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

193 cteroids and act as O(2) buffers, preventing nitrogenase inactivation; and Glb1-1 modulates nitric ox

194 Limited studies with the V- and Fe-nitrogenases initially demonstrated that these enzymes w

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 The nitrogenase iron protein (Fe-protein) contains an unusua

199 Nitrogenase is a key player in the global nitrogen cycle

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 an ATP-requiring enzyme capable of carryi

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

204 Binding of N(2) by the FeMo-cofactor of nitrogenase is believed to occur after transfer of 4 e(-

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

206 duction to two NH(3) molecules by the enzyme nitrogenase is E(4)(4H), the "Janus" intermediate, which

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

208 Nitrogenase is most commonly associated with the molybde

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 Nitrogenase is the enzyme that catalyzes biological N(2)

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

213 Nitrogenase is the only enzyme capable of reducing N(2)

214 Nitrogenase is the only enzyme that can convert atmosphe

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

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

217 s due to insufficient electron flux to the V-nitrogenase isoform on succinate compared with acetate.

218 es of diazotrophic growth based on different nitrogenase isoforms.

219 tion proteins, O(2) homeostasis systems, and nitrogenase itself.

220 and produce more byproduct H(2) than the Mo-nitrogenase, leading to an assumption that their usage r

221 g useful reference for reduced nitrogen in a nitrogenase-like environment.

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

223 pathway, present in numerous species, uses a nitrogenase-like reductase that is distinct from known n

224 that is distinct from known nitrogenases and nitrogenase-like reductases and specifically functions i

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

226 We show that coexpression in yeast of the nitrogenase maturation proteins NifU, NifS, and FdxN fro

227 obal biological nitrogen cycle and iron-only nitrogenase may contribute products that shape microbial

228 Recent work indicates that vanadium nitrogenase may play a role in the global biological nit

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

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

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

232 The electronic structure of the nitrogenase metal cofactors is central to nitrogen fixat

233 Formation of nitrogenase metalloclusters requires the participation o

234 bdenum (Mo), vanadium (V) and iron (Fe)-only nitrogenase metalloenzymes.

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

236 The active site of the nitrogenase MoFe protein corresponds to a [MoFe(7)S(9)C-

237 Coupling the nitrogenase MoFe protein to light-harvesting semiconduct

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

239 hereby facilitating electron transfer to the nitrogenase molybdenum iron-protein.

240 ort a 1.83-angstrom crystal structure of the nitrogenase molybdenum-iron (MoFe) protein captured unde

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

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

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

244 hown to limit BNF by the most common form of nitrogenase (Nase), which requires Mo in its active site

245 lineages have been detected based on partial nitrogenase (nifH) gene sequences, including the four mo

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

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

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

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

250 itrogenase supports growth as fast as the Mo-nitrogenase on acetate but not on the more oxidized subs

251 espite slightly faster growth based on the V-nitrogenase on acetate, the wild-type strain uses exclus

252 the wild-type strain uses exclusively the Mo-nitrogenase on both carbon substrates.

253 rogel to immobilize the catalytic protein of nitrogenase onto an electrode surface.

254 ificant advances in our understanding of how nitrogenase orchestrates electron transfer (ET) from the

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

256 us fertilizer and low oxygen, but continuous nitrogenase production confers an energy burden.

257 onia and hydrazine, demonstrating that these nitrogenase products can be generated from N(2) at a syn

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

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

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

261 Nitrogenase reduces dinitrogen (N2) to ammonia in biolog

262 itrogenase complex, illuminating the role of nitrogenase reductase in altering the potential landscap

263 The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving tw

264 fruitful, though key aspects about V- and Fe-nitrogenases remain unexplored.

265 Binding of N(2) by nitrogenase requires a reductive activation of the FeMo-

266 Moreover, a structure of V-dependent nitrogenase resulted in a proposed structure analogous t

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

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

269 asize the benefits of investigating multiple nitrogenase species.

270 d, and remaining challenges in understanding nitrogenase substrate reduction are considered.

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

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

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

274 The V-nitrogenase supports growth as fast as the Mo-nitrogenas

275 late 1980s and early 1990s, two "alternative nitrogenase" systems were discovered, isolated, and foun

276 by the plant is crucial for rhizobial enzyme nitrogenase that catalyses nitrogen fixation, but the SM

277 Alternative vanadium and iron-only nitrogenases that are homologous to molybdenum nitrogena

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

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

280 gher-order C(>=2) products is also known for nitrogenase, though potential metal-carbon multiply bond

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

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

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

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

285 core of the active-site cofactors for all 3 nitrogenase types.

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

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

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

289 The enzyme nitrogenase uses a suite of complex metallocofactors to

290 e, we elucidate the contribution of vanadium nitrogenase (V-Nase) to BNF by cyanolichens across a 600

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

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

293 nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the cleavage of the relat

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

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

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

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

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

299 toward the assembly of the catalytic unit of nitrogenase within mitochondria.

300 The stable and efficient electric wiring of nitrogenase within the redox polymer matrix enables medi