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PMID: 1908693 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterization of a soluble ferric reductase from Neisseria gonorrhoeae.

Biology of metals ·Vol. 4 ·No. 2 ·1991-00-00 ·Pages 126-31

Le Faou AE, Morse SA

Abstract

An NADH-dependent ferric reductase was identified in extracts of Neisseria gonorrhoeae. Enzyme activity was measured in an assay using ferrozine as the ferrous iron acceptor. Ferric reductase activity was enhanced by Mg2+ and flavine nucleotides. The enzyme reduced both citrate- and diphosphate-bound ferric iron as well as ferric hydroxide (Imferon). However, no activity was observed with either 30%-iron-saturated transferrin or with the gonococcal iron-binding protein, Fbp. The ferric reductase was found primarily within the cytoplasmic cell fraction. The soluble ferric reductase was purified 110-fold by ammonium sulfate precipitation, gel and anion-exchange chromatography. Results obtained following gel chromatography and SDS/polyacrylamide gel electrophoresis suggested that the enzyme had a molecular mass of about 25 kDa.

MeSH Terms
Cell-Free System FMN Reductase Kinetics Molecular Weight NADH, NADPH Oxidoreductases/isolation & purification Neisseria gonorrhoeae/enzymology Oxidation-Reduction Solubility
Chemicals
FMN Reductase NADH, NADPH Oxidoreductases ferric citrate iron reductase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Le Faou A E
Division of Sexually Transmitted Diseases Laboratory Research, Centers for Disease Control, Atlanta, Georgia 30333.
Morse S A
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Article Info
Journal
Biology of metals
Abbr.
Biol Met
ISSN
0933-5854
DOI
10.1007/BF01135390
Published
1991-00-00
Pages
126-31
Language
English
Region
Germany
NLM ID
8915662
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01135390
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