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Titolo:
STRUCTURE OF THE NATIVE CYSTEINE-SULFENIC ACID REDOX CENTER OF ENTEROCOCCAL NADH PEROXIDASE REFINED AT 2.8 ANGSTROM RESOLUTION
Autore:
YEH JI; CLAIBORNE A; HOL WGJ;
Indirizzi:
UNIV WASHINGTON,HOWARD HUGHES MED INST,DEPT BIOL STRUCT,BIOMOL STRUCTCTR,BOX 357742 SEATTLE WA 98195 UNIV WASHINGTON,HOWARD HUGHES MED INST,DEPT BIOL STRUCT,BIOMOL STRUCTCTR SEATTLE WA 98195 WAKE FOREST UNIV,MED CTR,DEPT BIOCHEM WINSTON SALEM NC 27157
Titolo Testata:
Biochemistry
fascicolo: 31, volume: 35, anno: 1996,
pagine: 9951 - 9957
SICI:
0006-2960(1996)35:31<9951:SOTNCA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
STREPTOCOCCUS-FAECALIS 10C1; BINDING ACTIVITY INVITRO; CRYSTAL-STRUCTURE; TRANSCRIPTIONAL REGULATOR; ENZYME; OXIDATION; CATALYSIS; RESIDUE; SITE; REACTIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
J.I. Yeh et al., "STRUCTURE OF THE NATIVE CYSTEINE-SULFENIC ACID REDOX CENTER OF ENTEROCOCCAL NADH PEROXIDASE REFINED AT 2.8 ANGSTROM RESOLUTION", Biochemistry, 35(31), 1996, pp. 9951-9957

Abstract

In order to obtain the crystal structure of the flavoprotein NADH peroxidase with its native Cys42-sulfenic acid redox center, a strategy combining reduced exposure of crystals to ambient oxygen and data collection at -160 degrees C was applied, The structure of the native enzyme to 2.8 Angstrom resolution is described; these results conclusively establish the existence of the Cys42-sulfenic acid as the functional non-flavin redox center of the peroxidase and provide the first structure for any naturally occurring protein-sulfenic acid, The Cys42-sulfenic acid atoms C alpha-C beta-S gamma-O roughly define a planar arrangement which is stacked parallel to the si face of the FAD isoalloxazineand positions the sulfenyl oxygen atom only 3.3 Angstrom from FAD-C4A. His10-N epsilon 2 contributes a hydrogen bond to the sulfenic acid oxygen, at a distance of 3.2 Angstrom. Although one oxygen atom (OX1) of the non-native Cys42-sulfonic acid derivative identified in the earlier wild-type peroxidase structure was taken to represent the native Cys42-sulfenic acid oxygen [Stehle, T., Ahmed, S. A., Claiborne, A., & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344], this structure shows that the sulfenic acid oxygen does not occupy this position, nor isit hydrogen-bonded to Cys42-N as was OX1, Comparison of the native Cys42-sulfenic acid structure with that of two-electron reduced glutathione reductase provides an insight into the sulfenic acid FAD charge-transfer interaction observed with both wild-type and His10 mutant peroxidases, A model of the E . NADH intermediate recently observed in stopped-flow analyses of the enzyme [Crane, E. J., III, Parsonage, D., Poole, L. B., & Claiborne, A. (1995) Biochemistry 34, 14114-14124] has also been generated to assist in analyzing the chemical mechanism of sulfenic acid reduction.

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Documento generato il 19/01/20 alle ore 09:45:24