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A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: implications for the evolution of energy-conserving heme-copper oxidases

Authors :
Gronberg, Karin L.C.
Roldan, M. Dolores
Prior, Louise
Butland, Gareth
Cheesman, Myles R.
Richardson, David J.
Spiro, Stephen
Thomson, Andrew J.
Watmough, Nicholas J.
Source :
Biochemistry. Oct 19, 1999, Vol. 38 Issue 42, p13780, 7 p.
Publication Year :
1999

Abstract

The action of bacterial nitric oxide reductase (NOR) on nitric oxide and nitrous oxide plays an integral role in the completion of the two-electron process undergone by these compounds. NOR is considered a diverged member of the heme-copper oxidase group since it exhibits a distinct electronic absorption spectrum. Experimental data derived from a Pavacocus denitrificans strain suggest that the oxygen reducing activity manifested by heme-copper oxidases is significantly attributed to the substitution of copper for non-heme iron in the dinuclear center.

Details

ISSN :
00062960
Volume :
38
Issue :
42
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.57796220