Journal article
Rieske business: Structure–function of Rieske non-heme oxygenases
Biochemical and biophysical research communications, Vol.338(1), pp.175-190
12/09/2005
DOI: 10.1016/j.bbrc.2005.08.222
PMID: 16168954
Abstract
Rieske non-heme iron oxygenases (RO) catalyze stereo- and regiospecific reactions. Recently, an explosion of structural information on this class of enzymes has occurred in the literature. ROs are two/three component systems: a reductase component that obtains electrons from NAD(P)H, often a Rieske ferredoxin component that shuttles the electrons and an oxygenase component that performs catalysis. The oxygenase component structures have all shown to be of the α
3 or α
3β
3 types. The transfer of electrons happens from the Rieske center to the mononuclear iron of the neighboring subunit via a conserved aspartate, which is shown to be involved in gating electron transport. Molecular oxygen has been shown to bind side-on in naphthalene dioxygenase and a concerted mechanism of oxygen activation and hydroxylation of the ring has been proposed. The orientation of binding of the substrate to the enzyme is hypothesized to control the substrate selectivity and regio-specificity of product formation.
Details
- Title: Subtitle
- Rieske business: Structure–function of Rieske non-heme oxygenases
- Creators
- Daniel J. Ferraro - University of IowaLokesh Gakhar - University of IowaS. Ramaswamy - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Biochemical and biophysical research communications, Vol.338(1), pp.175-190
- Publisher
- Elsevier Inc
- DOI
- 10.1016/j.bbrc.2005.08.222
- PMID
- 16168954
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Language
- English
- Date published
- 12/09/2005
- Academic Unit
- Medicine Administration
- Record Identifier
- 9984622049802771
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