Chemical Reviews· 2014Q1· Review
Heme Enzyme Structure and Function
- 1,402citations
- Q1SCImago
- 2014year
Short summary
Heme enzymes catalyze oxidation reactions using either O2 or H2O2, with O2 being a surprisingly unusual oxidant due to its paramagnetic nature creating a spin-forbidden reaction barrier.
AI-generated from the title and abstract; the full text is not read.
Key points
- Heme enzymes are categorized into oxygenases (using O2) and peroxidases (using H2O2).
- Crystal structures are available for the reviewed enzymes.
- Molecular oxygen (O2) is an unusual oxidant because it is paramagnetic.
- The paramagnetic nature of O2 creates a spin-forbidden reaction barrier with most biological molecules.
AI-generated from the title and abstract; the full text is not read.
Abstract
The review focuses on those enzymes that catalyze oxidation reactions and those for which crystal structures are available. There are two broad classes of heme enzyme oxidants: oxygenases that use O2 to oxidize, oxygenate, substrates and peroxidases that use 2O2 to oxidize. The review demonstrates that out of the oxidants molecular oxygen is the most unusual, as O2 is not a reactive molecule despite the oxidation of nearly all biological molecules by O2 being a thermodynamically favorable process. The reason is that there is a large kinetic barrier to these reactions owing to O2 being a paramagnetic molecule so that the reaction between a majority of biological molecules that have paired spins is a spin forbidden process.
The authors' abstract, as published at the source. Chemical Reviews, 2014 · DOI ↗
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Field: Inorganic Chemistry
Inorganic ChemistryChemistry