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Literature summary for 1.18.6.1 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
Search for more literature for 1.18.6.1

Inhibitors

Inhibitors Comment Organism Structure
O2 irreversibly inactivated Cyanobacterium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum
-
 Trichormus variabilis
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Trichormus variabilis
-
 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
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
-
 ?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Cyanobacterium sp. regulation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
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

Organism UniProt Comment Textmining
Cyanobacterium sp.
-
-
-
Trichormus variabilis
-
-
-

Oxidation Stability

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

Reaction

Reaction Comment Organism Reaction ID
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
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Cyanobacterium sp. 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Trichormus variabilis 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
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
-
 ?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O regulation Cyanobacterium sp. 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
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

Subunits Comment Organism
tetramer
-
 Cyanobacterium sp.