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Volumn 286, Issue 13, 2011, Pages 11849-11854

A twin-track approach has optimized proton and hydride transfer by dynamically coupled tunneling during the evolution of protochlorophyllide oxidoreductase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED ENZYMES; ACTIVE SITE; CATALYTIC POWER; CATALYTIC STRUCTURE; COUPLED DYNAMICS; DYNAMIC EFFECTS; DYNAMIC PROPERTY; ENZYME CATALYSIS; EVOLUTIONARY ORIGIN; FUNCTIONAL ADAPTATION; HYDRIDE TRANSFERS; ISOTOPE EFFECT; PLANT ENZYMES; PROTEIN DYNAMICS; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; PROTON DONORS; TEMPERATURE DEPENDENCE; THERMALLY ACTIVATED;

EID: 79953218084     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.219626     Document Type: Article
Times cited : (26)

References (34)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.