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. 1985 Oct;164(1):316–320. doi: 10.1128/jb.164.1.316-320.1985

Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas.

D J Klemm, L L Barton
PMCID: PMC214246  PMID: 4044523

Abstract

The anaerobic oxidation of protoporphyrinogen to protoporphyrin was demonstrated in extracts of Desulfovibrio gigas. Protoporphyrin formation occurred in the presence of nitrite, hydroxylamine, sulfite, thiosulfate, ATP plus sulfate, NAD+, NADP+, flavin adenine dinucleotide, flavin mononucleotide, fumarate, 2,6-dichlorophenol-indophenol, methyl viologen, and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. With dialyzed cell extracts, highest activities were observed with sulfite, NAD+, and NADP+ as electron acceptors. The enzyme for protoporphyrinogen oxidation was localized in the membrane of D. gigas and displayed optimal activity at pH 7.3 and 28 degrees C.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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