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Volumn 112, Issue 48, 2008, Pages 15478-15486

Major Mo(V) EPR signature of rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSTS; DIMETHYL SULFOXIDE; ELECTRON RESONANCE; ENZYME ACTIVITY; ENZYMES; MOLYBDENUM; NITRATES; PARAMAGNETIC RESONANCE; PROTEINS; QUANTUM THEORY; VOLTAMMETRY;

EID: 57949107626     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp807092y     Document Type: Article
Times cited : (45)

References (45)
  • 2
    • 0000273676 scopus 로고    scopus 로고
    • Hille, R. Chem. Rev. 1996, 96, 2757-2816.
    • (1996) Chem. Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 33
    • 84906383258 scopus 로고    scopus 로고
    • An activation faster than about Is would be masked by the charging current, whereas very slow activation could be hidden by the decrease in current resulting from film desorption, which occurs under these conditions with first-order kinetics and a characteristic time of about 3000 s
    • An activation faster than about Is would be masked by the charging current, whereas very slow activation could be hidden by the decrease in current resulting from film desorption, which occurs under these conditions with first-order kinetics and a characteristic time of about 3000 s.
  • 34
    • 84906412171 scopus 로고    scopus 로고
    • -1.
    • -1.
  • 36
    • 84906383259 scopus 로고    scopus 로고
    • As opposed to electrochemically poised using protein film voltammetry
    • As opposed to electrochemically poised using protein film voltammetry.
  • 37
    • 84906383256 scopus 로고    scopus 로고
    • 38
    • 38


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.