IntEnz Enzyme Nomenclature
EC 1.18.6.1
Names
Accepted name:
nitrogenase
Other
name:
reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing)
Systematic name:
ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing, molybdenum-dependent)
Reaction
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cofactors
Comments:
Requires Mg2+. The enzyme is a complex of two components (namely dinitrogen reducatse and dinitrogenase). Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component. Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine. The reduction is initiated by formation of hydrogen in stoichiometric amounts [2]. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)]. The enzyme does not reduce CO (cf. EC 1.18.6.2, vanadium-dependent nitrogenase).
Links to other databases
CAS Registry Number:
9013-04-1
ANFD_AZOVI
ANFD_HELGE
ANFD_RHOCA
ANFD_RUMHU
ANFG_AZOMA
ANFG_AZOPA
ANFG_AZOVI
ANFG_CLOPA
ANFG_RHOCA
ANFG_RHORU
ANFG_RUMHU
ANFK_AZOVI
ANFK_RHOCA
ANFK_RUMHU
NIFD_ACIFI
NIFD_ALCFA
NIFD_ANASL
NIFD_AZOBR
NIFD_AZOVI
NIFD_BRADU
NIFD_BRASP
NIFD_CLOPA
NIFD_CROS5
NIFD_FRAAL
NIFD_HERSE
NIFD_KLEPN
NIFD_LEPBY
NIFD_METBA
NIFD_METIV
NIFD_METMI
NIFD_METMP
NIFD_METTH
NIFD_METTL
NIFD_METTM
NIFD_NOSCO
NIFD_NOSS1
NIFD_RHICP
NIFD_RHILT
NIFD_RHOCA
NIFD_RIPO1
NIFD_SINFN
NIFH1_AZOC5
NIFH1_AZOCH
NIFH1_AZOVI
NIFH1_CLOPA
NIFH1_MASLA
NIFH1_METBA
NIFH1_METIV
NIFH1_METTH
NIFH1_METTL
NIFH1_METTM
NIFH1_NOSS1
NIFH1_PAEDU
NIFH1_RHOCA
NIFH1_RHOCB
NIFH1_TRIV2
NIFH2_AZOC5
NIFH2_AZOCH
NIFH2_AZOVI
NIFH2_CLOPA
NIFH2_MASLA
NIFH2_METBA
NIFH2_METIV
NIFH2_METTH
NIFH2_METTL
NIFH2_NOSS1
NIFH2_PAEDU
NIFH2_RHOCA
NIFH2_TRIV2
NIFH3_AZOVI
NIFH3_CLOPA
NIFH4_CLOPA
NIFH5_CLOPA
NIFH6_CLOPA
NIFH_ACIF2
NIFH_ACIF5
NIFH_ACIFR
NIFH_ALCFA
NIFH_ALKMQ
NIFH_ANASL
NIFH_AZOBR
NIFH_AZOPC
NIFH_BRADU
NIFH_BRASP
NIFH_CERS4
NIFH_CERSP
NIFH_CHLCH
NIFH_CHLL2
NIFH_CHLL3
NIFH_CHLP8
NIFH_CHLPB
NIFH_CHLPD
NIFH_CHLPM
NIFH_CHLTE
NIFH_CLOAB
NIFH_CROS5
NIFH_CYAP4
NIFH_DECAR
NIFH_DEHM1
NIFH_DESAH
NIFH_DESAL
NIFH_DESAP
NIFH_DESGI
NIFH_DESMC
NIFH_DESMR
NIFH_DESRM
NIFH_ENTAG
NIFH_FRAAL
NIFH_FRACC
NIFH_FRASE
NIFH_FRASN
NIFH_FRASP
NIFH_GLOC7
NIFH_GLUDA
NIFH_HERSE
NIFH_KLEP3
NIFH_KLEPN
NIFH_LEPBY
NIFH_MAGMM
NIFH_MARSD
NIFH_METAR
NIFH_METHJ
NIFH_METJA
NIFH_METMA
NIFH_METMI
NIFH_METMJ
NIFH_METMP
NIFH_METNO
NIFH_METS4
NIFH_METVO
NIFH_NOSCO
NIFH_NOSS6
NIFH_NOSSN
NIFH_PECAS
NIFH_PELPB
NIFH_PROA2
NIFH_PSEU5
NIFH_RHIET
NIFH_RHILE
NIFH_RHILO
NIFH_RHILT
NIFH_RHIME
NIFH_RHOP2
NIFH_RHOPS
NIFH_RHORU
NIFH_RHOS1
NIFH_RIPO1
NIFH_ROSCS
NIFH_ROSS1
NIFH_RUMCE
NIFH_SINFN
NIFH_SYNFM
NIFH_SYNJA
NIFH_SYNJB
NIFH_TERTT
NIFH_TOLAT
NIFH_TRIAZ
NIFH_TRIEI
NIFH_TRITH
NIFH_WOLSU
NIFH_ZYMMO
NIFK_ACIFI
NIFK_AZOBR
NIFK_AZOVI
NIFK_BRADU
NIFK_BRASP
NIFK_CLOPA
NIFK_CROS5
NIFK_FRAAL
NIFK_HERSE
NIFK_KLEPN
NIFK_METBA
NIFK_METMI
NIFK_METMP
NIFK_METTH
NIFK_METTL
NIFK_METTM
NIFK_NOSS1
NIFK_RIPO1
NIFK_SINFN
VNFD_AZOCH
VNFD_AZOPA
VNFD_AZOSA
VNFD_AZOVI
VNFG_AZOCH
VNFG_AZOSA
VNFG_AZOVI
VNFK_AZOCH
VNFK_AZOPA
VNFK_AZOSA
VNFK_AZOVI
VNFK_TRIV2
References
-
Zumft, W.G., Paneque, A., Aparicio, P.J. and Losada, M.
Mechanism of nitrate reduction in Chlorella.
Biochem. Biophys. Res. Commun.
36
:
980-986
(1969).
[PMID:
4390523]
-
Liang, J. and Burris, R.H.
Hydrogen burst associated with nitrogenase-catalyzed reactions.
Proc. Natl. Acad. Sci. USA
85
:
9446-9450
(1989).
[PMID:
3200830]
-
Dance, I.
The mechanism of nitrogenase. Computed details of the site and geometry of binding of alkyne and alkene substrates and intermediates.
J. Am. Chem. Soc.
126
:
11852-11863
(2004).
[PMID:
15382920]
-
Chan, J.M., Wu, W., Dean, D.R. and Seefeldt, L.C.
Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis.
Biochemistry
39
:
7221-7228
(2000).
[PMID:
10852721]
[EC 1.18.6.1 created 1978 as EC 1.18.2.1, transferred 1984 to EC 1.18.6.1, modified 2005, modified 2018]