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- W2987696353 endingPage "1307" @default.
- W2987696353 startingPage "1286" @default.
- W2987696353 abstract "Iron–porphyrins ([Formula: see text] hemes) are present throughout the biosphere and perform a wide range of functions, particularly those that involve complex multiple-electron redox processes. Some common heme enzymes involved in these processes include cytochrome P450, heme/copper oxidase or heme/non-heme diiron nitric oxide reductase. Consequently, the (hydr)oxo-bridged heme species have been studied for the important roles that they play in many life processes or for their application for catalysis and preparation of new functional materials. This review encompasses important synthetic, structural and reactivity aspects of the (hydr)oxo-bridged heme constructs that govern their function and application. The properties and reactivity of the bridging (hydr)oxo moieties are directly dictated by the coordination environment of the heme core, the nature and ligation of the second metal center attached to the (hydr)oxo group, the presence or absence of a linker, and the degree of flexibility around that linker within the scaffold. Here, we summarize the structural features of all known (hydr)oxo-bridged heme constructs and use those to categorize and thus, provide a more comprehensive picture of structure–function relationships." @default.
- W2987696353 created "2019-11-22" @default.
- W2987696353 creator A5038414426 @default.
- W2987696353 creator A5049624006 @default.
- W2987696353 date "2019-12-01" @default.
- W2987696353 modified "2023-10-18" @default.
- W2987696353 title "(Hydr)oxo-bridged heme complexes: From structure to reactivity" @default.
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