Please use this identifier to cite or link to this item: 192.168.6.56/handle/123456789/76334
Full metadata record
DC FieldValueLanguage
dc.contributor.advisorR. BITTMAN-
dc.contributor.advisorN. BORGESE-
dc.contributor.advisorD. DASGUPTA-
dc.contributor.advisorH. ENGELHARDT-
dc.contributor.advisorA.-H. ETEMADI-
dc.contributor.advisorS. FULLER-
dc.contributor.advisorJ. HACKER-
dc.contributor.advisorH. HERRMANN-
dc.contributor.advisorJ. B. LLOYD-
dc.contributor.advisorP. QUINN,-
dc.contributor.advisorS. ROTTEM-
dc.contributor.editorHolzenburg, Andreas-
dc.contributor.editorS. Scrutton, Nigel-
dc.date.accessioned2019-07-23T10:52:42Z-
dc.date.available2019-07-23T10:52:42Z-
dc.date.issued2002-
dc.identifier.isbn0-306-46828-X-
dc.identifier.urihttp://10.6.20.12:80/handle/123456789/76334-
dc.descriptionMajor advances have been made in recent years in the field of redox enzy- mology. In part this has been attributable to the wealth of structural infor- mation acquired for redox systems, principally by X-ray methods. The successful application of electron transfer theory to redox proteins has also put the study of biological electron transfer onto a sound theoretical plat- form. Coupled with the ability to interrogate mechanism by site-directed mutagenesis, spectroscopic and transient kinetic methods these develop- ments have contributed to the major expansion seen in recent years of research activity in the field of biological electron and radical transfer.en
dc.languageenen
dc.language.isoenen_US
dc.publisherKluwer Academicen_US
dc.subjectEnzyme-Catalyzed Electron and Radical Transferen_US
dc.titleEnzyme-Catalyzed Electron and Radical Transferen_US
dc.typeBooken_US
Appears in Collections:Chemistry

Files in This Item:
File Description SizeFormat 
3.pdf6.66 MBAdobe PDFView/Open
Show simple item record


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.