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Q35377798-0272EB49-4F3E-496C-B43D-D650FAC8B4FC
Q35377798-0272EB49-4F3E-496C-B43D-D650FAC8B4FC
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http://www.wikidata.org/entity/statement/Q35377798-0272EB49-4F3E-496C-B43D-D650FAC8B4FC
The entropic contributions in vitamin B12 enzymes still reflect the electrostatic paradigm.
P2860
Q35377798-0272EB49-4F3E-496C-B43D-D650FAC8B4FC
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35377798-0272EB49-4F3E-496C-B43D-D650FAC8B4FC
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b1a9b2f458df413866a6b8d789adb77b2e178305
P2860
Role of active site residues in promoting cobalt-carbon bond homolysis in adenosylcobalamin-dependent mutases revealed through experiment and computation.