Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and ac-type cytochrome
Author:
Funder
NSF
USPHS
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560020203/fullpdf
Reference32 articles.
1. Electron-tunneling pathways in ruthenated proteins;Beratan;J. Am. Chem. Soc.,1990
2. Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin;Chen;Biochemistry,1992a
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1. Amicyanin and Complexes of Amicyanin with Methylamine Dehydrogenase and Cytochromec551i;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15
2. Amicyanin Transfers Electrons from Methylamine Dehydrogenase to Cytochrome c-551i via a Ping-Pong Mechanism, not a Ternary Complex;Journal of the American Chemical Society;2010-09-27
3. Structural Comparison of Crystal and Solution States of the 138 kDa Complex of Methylamine Dehydrogenase and Amicyanin from Paracoccus versutus;Biochemistry;2008-05-31
4. Amicyanin and Complexes of Amicyanin with Methylamine Dehydrogenase and Cytochromec551i;Handbook of Metalloproteins;2006-04-15
5. Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2003-04
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