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Literature summary for 1.9.6.1 extracted from

  • Cerqueira, N.M.; Fernandes, P.A.; Gonzalez, P.J.; Moura, J.J.; Ramos, M.J.
    The sulfur shift an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase (2013), Inorg. Chem., 52, 10766-10772 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure analysis, resolution 2.2 A, PDB ID 2jio, modelling Desulfovibrio desulfuricans

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Desulfovibrio desulfuricans
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the heme/cytochrome cofactor Desulfovibrio desulfuricans
Mo(VI) coordinates a cysteine and a sulfido residue Desulfovibrio desulfuricans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferrocytochrome + 2 H+ + nitrate Desulfovibrio desulfuricans
-
2 ferricytochrome + nitrite
-
?

Organism

Organism UniProt Comment Textmining
Desulfovibrio desulfuricans P81186
-
-

Reaction

Reaction Comment Organism Reaction ID
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling Desulfovibrio desulfuricans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferrocytochrome + 2 H+ + nitrate
-
Desulfovibrio desulfuricans 2 ferricytochrome + nitrite
-
?

Synonyms

Synonyms Comment Organism
NAP
-
Desulfovibrio desulfuricans
periplasmic nitrate reductase
-
Desulfovibrio desulfuricans

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
Desulfovibrio desulfuricans
molybdenum cofactor a Mo-pyranopterin cofactor Desulfovibrio desulfuricans

General Information

General Information Comment Organism
evolution the periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans belongs to the DMSO reductase family, subfamily I. Classification of Mo-pyranopterin dependent enzymes from the DMSO reductase family, e.g. periplasmic nitrate reductase and formate dehydrogenase, overview. Comparison of the sulfur-shift mechanism in nitrate reductase (Nap) and in formate dehydrogenase (Fdh), detailed overview Desulfovibrio desulfuricans