Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 34, Issue 10, Pages 790-797Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar000184m
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- NIGMS NIH HHS [GM-46695] Funding Source: Medline
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Seven proton transfers in five steps participate in a catalytic turnover of an aspartic protease. The Rosetta Stone for elucidating their role is a low-barrier hydrogen bond that holds the two aspartic carboxyls in a coplanar conformation. The proton of this bond shuttles between oxygens during chemical steps via hydrogen tunneling, unlike in previous proposals where it was transferred to substrate. After the release of products, both carboxyls are protonated and the bond is missing. Re-forming the bond is a significant step within a kinetic isomechanism. The bond also explains-at long last-the extremely low pK in pH profiles.
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