Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms
- 1 April 1982
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 156 (2) , 389-409
- https://doi.org/10.1016/0022-2836(82)90335-7
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Conformation change of cytochrome cJournal of Molecular Biology, 1981
- Structure of actinidin, after refinement at 1.7 Å resolutionJournal of Molecular Biology, 1980
- pH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1980
- Thermodynamics of metalloprotein electron transfer reactionsPublished by Walter de Gruyter GmbH ,1980
- Dynamic information from protein crystallographyJournal of Molecular Biology, 1979
- Structure of erythrocruorin in different ligand states refined at 1·4 Å resolutionJournal of Molecular Biology, 1979
- Cytochrome oxidase from Pseudomonas aeruginosa. II. Reaction with copper proteinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- STUDIES ON THE CONFORMATION OF AMINO ACIDSInternational Journal of Protein Research, 1971
- Crystalline pseudomonas cytochrome oxidaseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- Studies on Cytochrome c. I. Electrophoretic Purification of Cytochrome c and its Amino Acid Composition*Journal of the American Chemical Society, 1941