Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 34, 2005, Pages 12041-12046

  Antonyuk, Svetlana V ^a   Strange, Richard W ^a   Sawers, Gary ^b   Eady, Robert R ^a   Hasnain, S Samar ^a  

^a DARESBURY LABORATORY   (United Kingdom)

^b JOHN INNES CENTRE   (United Kingdom)

Author keywords

Catalysis; Crystal structures; Denitrification; Enzyme mechanism; Nitrite and nitric oxide binding

Indexed keywords

NITRITE REDUCTASE;

ACHROMOBACTER CYCLOCLASTES; ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DENITRIFICATION; ECOSYSTEM; ENZYME MECHANISM; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SOIL MICROFLORA; STEADY STATE; STRUCTURE ANALYSIS;

ACHROMOBACTER CYCLOCLASTES; CATALYSIS; CRYSTALLIZATION; MODELS, MOLECULAR; NITRIC OXIDE; NITRITE REDUCTASES; OXIDATION-REDUCTION; SUBSTRATE SPECIFICITY;

ACHROMOBACTER CYCLOCLASTES; BACTERIA (MICROORGANISMS); FUNGI;

EID: 24744467360     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0504207102     Document Type: Article

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