fulltext.study @t Gmail

Artificial hydrogenases

Paper ID Volume ID Publish Year Pages File Format Full-Text
16006 42481 2010 6 PDF Available
Title
Artificial hydrogenases
Abstract

Decades of biophysical study on the hydrogenase (H2ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H2ases, [NiFe]-H2ases, and [Fe]-H2ases, all of which feature iron centers bound to both CO and thiolate. Artificial H2ases affect the oxidation of H2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H2 toward biomimetic H2ases.

First Page Preview
Artificial hydrogenases
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us
Publisher
Database: Elsevier - ScienceDirect
Journal: Current Opinion in Biotechnology - Volume 21, Issue 3, June 2010, Pages 292–297
Authors
, , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us