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Literature summary extracted from

  • Houchins, J.P.
    The physiology and biochemistry of hydrogen metabolism in cyanobacteria (1984), Biochim. Biophys. Acta, 768, 227-255.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 O2 irreversibly inactivated Cyanobacterium sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Molybdenum
-
 Trichormus variabilis
1.18.6.1 Molybdenum enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex Cyanobacterium sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.6.1 60000
-
 Fe protein Cyanobacterium sp.
1.18.6.1 216000
-
 nitrogenase complex Cyanobacterium sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Trichormus variabilis
-
 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Cyanobacterium sp. ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Cyanobacterium sp. regulation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Cyanobacterium sp. biological N2 fixation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Cyanobacterium sp.
-
-
-
1.18.6.1 Trichormus variabilis
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.18.6.1 extreme sensitivity to O2 Cyanobacterium sp.
1.18.6.1 stable to O2, no loss in nitrogen fixation activity Trichormus variabilis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.6.1 4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein Trichormus variabilis
a
1.18.6.1 4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein Cyanobacterium sp.
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.6.1 heterocyst in heterocysteous cyanobacteria exclusive site of N2 fixation during aerobic growth Cyanobacterium sp.
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Cyanobacterium sp. 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Trichormus variabilis 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O regulation Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O biological N2 fixation Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.18.6.1 tetramer
-
 Cyanobacterium sp.