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Q35648424-0BA62B04-5681-42CE-87F2-E9D9A5B88861
Q35648424-0BA62B04-5681-42CE-87F2-E9D9A5B88861
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http://www.wikidata.org/entity/statement/Q35648424-0BA62B04-5681-42CE-87F2-E9D9A5B88861
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.
P2860
Q35648424-0BA62B04-5681-42CE-87F2-E9D9A5B88861
BestRank
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http://www.wikidata.org/entity/statement/Q35648424-0BA62B04-5681-42CE-87F2-E9D9A5B88861
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5503b95ece125c88973d808f5c05c86ed041a9dd
P2860
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.