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Volumn 129, Issue 37, 2007, Pages 11447-11458

The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: A Q-band 57Fe-ENDOR and HYSCORE study

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONIC STRUCTURE; HYDROGEN; IRON; LIGANDS; OXIDATION; PARAMAGNETIC RESONANCE;

EID: 35048857033     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja072592s     Document Type: Article
Times cited : (149)

References (76)
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    • ox (Figure 8) cannot be completely excluded, although it seems unlikely. Further evidence for our assignment could be obtained from analysis of the spin density on the CO and CN ligands of the H-cluster.
    • ox (Figure 8) cannot be completely excluded, although it seems unlikely. Further evidence for our assignment could be obtained from analysis of the spin density on the CO and CN ligands of the H-cluster.
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    • It should be noted that the most detailed ENDOR and Mössbauer experiments have been performed on hydrogenase II from C. pasteurianum of which no crystal structure is available. Up to now, however, no follow-up studies of any kind have been published on hydrogenase II. Also, we were not able to find a gene encoding for this hydrogenase in the genome databases e.g, UNI-PROT, Therefore, it cannot be completely excluded that hydrogenase II is an artifact, e.g. a partly denatured hydrogenase I enzyme. Since in the meantime hydrogenase I of C. pasteurianum has been characterized very well, it may be worthwhile to repeat the ENDOR and Mössbauer experiments on this enzyme to verify the reported 57Fe hyperfine values
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.