The Thermodynamics of Xanthine Oxidoreductase Catalysis
dc.contributor.author | Sanders, Stephen A. | en_US |
dc.contributor.author | Massey, Vincent | en_US |
dc.date.accessioned | 2009-07-10T19:11:18Z | |
dc.date.available | 2009-07-10T19:11:18Z | |
dc.date.issued | 1999-09-01 | en_US |
dc.identifier.citation | Sanders, Stephen A.; Massey, Vincent (1999). "The Thermodynamics of Xanthine Oxidoreductase Catalysis." Antioxidants & Redox Signaling 1(3): 371-379 <http://hdl.handle.net/2027.42/63356> | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/63356 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11229448&dopt=citation | en_US |
dc.description.abstract | ABSTRACT Xanthine oxidoreductase is a complex enzyme found in a wide range of organisms. Recent interest in this enzyme stems from its ability to produce reactive oxygen species under a range of conditions. It is found as a homodimer, each unit containing a molybdopterin cofactor, two iron sulfur centers, and FAD. The enzyme can exist in two forms that differ primarily in their oxidizing substrate specificity. The dehydrogenase form preferentially utilizes NAD+ as an electron acceptor but is able to donate electrons to molecular oxygen. Xanthine dehydrogenase from mammalian sources can be converted to an oxidase form that readily donates electrons to molecular oxygen, but does not reduce NAD+. The catalytic mechanism of both forms of the enzyme can be described in terms of a rapid equilibrium model in which reducing equivalents are distributed rapidly between the different redox centers of the enzyme on the basis of their midpoint potentials. The present commentary gives a brief overview of the literature concerning the rapid equilibrium model and the differences between the two enzyme forms. NADH is also discussed in terms of an alternative to xanthine or hypoxanthine as an electron donor. | en_US |
dc.format.extent | 262025 bytes | |
dc.format.extent | 2489 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Mary Ann Liebert, Inc., publishers | en_US |
dc.title | The Thermodynamics of Xanthine Oxidoreductase Catalysis | en_US |
dc.type | Article | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 11229448 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/63356/1/ars.1999.1.3-371.pdf | |
dc.identifier.doi | doi:10.1089/ars.1999.1.3-371 | en_US |
dc.identifier.source | Antioxidants & Redox Signaling | en_US |
dc.identifier.source | Antioxidants & Redox Signaling | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.