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http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_43/101021bi00043a017/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/1995/volume_117/issue_40/101021ja00145a048/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_18/101021ja029420/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_2/101021ja044365l/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1995/volume_117/issue_26/101021ja00131a039/authorship/4
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Structural and electronic similarity but functional difference in methylmalonyl-CoA mutase between coenzyme B12 and the analog 2,'5'-dideoxyadenosylcobalamin
Coenzyme B12 Is Coordinated by Histidine and Not Dimethylbenzimidazole on Methylmalonyl-CoA Mutase. [Erratum to document cited in CA123:78304]
Tyrosine 89 Accelerates Co−Carbon Bond Homolysis inMethylmalonyl-CoA Mutase
Mirror “Base-off” Conformation of Coenzyme B12 in HumanAdenosyltransferase and Its Downstream Target, Methylmalonyl-CoA Mutase
Coenzyme B12 Is Coordinated by Histidine and Not Dimethylbenzimidazole on Methylmalonyl-CoA Mutase
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