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Volumn 47, Issue 16, 2008, Pages 7405-7414

Redox and structural properties of mixed-valence models for the active site of the [FeFe]-hydrogenase: Progress and challenges

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDE; DRUG DERIVATIVE; HYDROGENASE; IRON HYDROGENASE; IRON SULFUR PROTEIN; LIGAND; PROPANE; PROPANEDITHIOLATE; THIOL DERIVATIVE;

EID: 50449103696     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic8007552     Document Type: Article
Times cited : (98)

References (40)
  • 25
    • 50449103054 scopus 로고    scopus 로고
    • +, evaluating the possible presence of low-lying excited states in which the unpaired electron is not localized on the Fe atom featuring vacant apical coordination site. We found that the lowest-energy excited state is about 23 kcal/mol higher in energy than the ground state. More importantly, in the excited state the spin density distribution was largely unaffected.
    • +, evaluating the possible presence of low-lying excited states in which the unpaired electron is not localized on the Fe atom featuring vacant apical coordination site. We found that the lowest-energy excited state is about 23 kcal/mol higher in energy than the ground state. More importantly, in the excited state the spin density distribution was largely unaffected.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.