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Article

Molybdoenzyme biosynthesis in Escherichia coli: in vitro activation of purified nitrate reductase from a chlB mutant.

Journal of bacteriology - 1 Dec 1992

Santini C L, Iobbi-Nivol C, Romane C, Boxer D H, Giordano G

Abstract excerpt

All molybdoenzyme activities are absent in chlB mutants because of their inability to synthesize molybdopterin guanine dinucleotide, which together with molybdate constitutes the molybdenum cofactor in Escherichia coli. The chlB mutants are able to synthesize molybdopterin. We have previously shown that the inactive nitrate reductase present in a chlB mutant can be activated in a process requiring protein FA and...

Topics

Bacterial Proteins
Chlorates
Coenzymes
Drug Resistance, Microbial
Enzyme Activation
Escherichia coli
Guanosine Triphosphate
Kinetics
Metalloproteins
Molecular Weight
Molybdenum Cofactors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nitrate Reductase

Nitrate Reductases

Pteridines

Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 1459941
DOI: 10.1128/jb.174.24.7934-7940.1992
PMCID: PMC207528

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1459941-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Molybdoenzyme biosynthesis in Escherichia coli: in vitro activation of purified nitrate reductase from a chlB mutant.PMID 1459941Read ↗

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