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. 1983 Apr;154(1):387–394. doi: 10.1128/jb.154.1.387-394.1983

Escherichia coli nitrate reductase subunit A: its role as the catalytic site and evidence for its modification.

G R Chaudhry, C H MacGregor
PMCID: PMC217471  PMID: 6403509

Abstract

Subunits A and B were isolated from purified nitrate reductase by preparative electrophoresis in low levels of sodium dodecyl sulfate. Nonheme iron and low levels of molybdenum were associated with isolated subunit A but not with isolated subunit B. After dialysis against a source of molybdenum cofactor, subunit A regained tightly bound molybdenum and concomitantly regained enzyme activity and reactivity with anti-nitrate reductase antiserum. Subunit B neither bound cofactor nor regained activity or reactivity with antiserum. These data indicate that subunit A contains the active site of the enzyme. Subunit A was also found to be modified posttranslationally in a similar fashion as is subunit B. This was determined by comparison of partial proteolytic digests and amino acid analyses of A subunits from precursor and membrane-bound forms of nitrate reductase.

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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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