How do enzymes activate oxygen without inactivating themselves?
Detailed analyses of the oxidative half-reactions of glucose oxidase and soybean lipoxygenase provide insight into Nature's solution to the "trouble with oxygen". Coupled with studies of other O2-activating enzymes, two key features emerge. The first is the predominance of a rate-limiting transfer of the first electron transfer to O2, with subsequent electron and proton transfers occurring in rapid steps. The second feature is the identification of non-metal binding sites and channels for O2. These permit a controlled reactivity of oxygen to generate the desired regio- and stereochemical products, while minimizing deleterious side reactions.
Klinman
Judith P
JP
Department of Chemistry, University of California, Berkeley, California 94720, USA. klinman@berkeley.edu
D001665:Binding Sites; D004579:Electron Transport; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008084:Lipoxygenase / Q000737:chemistry / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D012997:Solvents / Q000737:chemistry; D013025:Glycine max / Q000201:enzymology; D013237:Stereoisomerism
D011522:Protons; D012997:Solvents; D005949:Glucose Oxidase; D008084:Lipoxygenase; D010100:Oxygen