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Liang, N., Pielak, G. J., Mauk, A. G., Smith, M., Hoffman, B. M. (1987) Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences, 84 (5) 1249-1252 doi:10.1073/pnas.84.5.1249

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Reference TypeJournal (article/letter/editorial)
TitleYeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants.
JournalProceedings of the National Academy of Sciences
AuthorsLiang, N.Author
Pielak, G. J.Author
Mauk, A. G.Author
Smith, M.Author
Hoffman, B. M.Author
Year1987 (March 1)Volume84
Issue5
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.84.5.1249Search in ResearchGate
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Mindat Ref. ID1463630Long-form Identifiermindat:1:5:1463630:1
GUID0
Full ReferenceLiang, N., Pielak, G. J., Mauk, A. G., Smith, M., Hoffman, B. M. (1987) Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences, 84 (5) 1249-1252 doi:10.1073/pnas.84.5.1249
Plain TextLiang, N., Pielak, G. J., Mauk, A. G., Smith, M., Hoffman, B. M. (1987) Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences, 84 (5) 1249-1252 doi:10.1073/pnas.84.5.1249
In(1987, March) Proceedings of the National Academy of Sciences Vol. 84 (5) Proceedings of the National Academy of Sciences

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Liang, N, Mauk, A., Pielak, G., Johnson, J., Smith, M, Hoffman, B. (1988) Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science, 240 (4850). 311-313 doi:10.1126/science.2832950
Goodin, D. B., Mauk, A. G., Smith, M. (1986) Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis. Proceedings of the National Academy of Sciences, 83 (5) 1295-1299 doi:10.1073/pnas.83.5.1295
Cheung, E., Taylor, K., Kornblatt, J. A., English, A. M., McLendon, G., Miller, J. R. (1986) Direct measurements of intramolecular electron transfer rates between cytochrome c and cytochrome c peroxidase: effects of exothermicity and primary sequence on rate. Proceedings of the National Academy of Sciences, 83 (5) 1330-1333 doi:10.1073/pnas.83.5.1330
ten Kortenaar, P. B., Adams, P. J., Tesser, G. I. (1985) Semisynthesis of horse heart cytochrome c analogues from two or three fragments. Proceedings of the National Academy of Sciences, 82 (24) 8279-8283 doi:10.1073/pnas.82.24.8279
Everest, Andrew M., Wallin, Sten A., Stemp, Eric D. A., Nocek, Judith M., Mauk, A. G., Hoffman, Brian M. (1991) Aromatic hole superexchange through position 82 of cytochrome c is not required for intracomplex electron transfer to zinc cytochrome c peroxidase. Journal Of The American Chemical Society, 113 (11) 4337-4338 doi:10.1021/ja00011a050
PIELAK, G. J., OIKAWA, K., MAUK, A. G., SMITH, M., KAY, C. M. (1986) ChemInform Abstract: Elimination of the Negative Soret Cotton Effect of Cytochrome c by Replacement of the Invariant Phenylalanine Using Site-Directed Mutagenesis. Chemischer Informationsdienst, 17 (37) doi:10.1002/chin.198637061
Schwartzman, M. L., Balazy, M., Masferrer, J., Abraham, N. G., McGiff, J. C., Murphy, R. C. (1987) 12(R)-hydroxyicosatetraenoic acid: a cytochrome-P450-dependent arachidonate metabolite that inhibits Na+,K+-ATPase in the cornea. Proceedings of the National Academy of Sciences, 84 (22) 8125-8129 doi:10.1073/pnas.84.22.8125
Lange, C., Hunte, C. (2002) Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proceedings of the National Academy of Sciences, 99 (5) 2800-2805 doi:10.1073/pnas.052704699
Hoffman, B. M., Roberts, J. E., Brown, T. G., Kang, C. H., Margoliash, E. (1979) Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster. Proceedings of the National Academy of Sciences, 76 (12) 6132-6136 doi:10.1073/pnas.76.12.6132
Nocek, Judith M., Liang, Nong, Wallin, Sten A., Mauk, A. Grant, Hoffman, Brian M. (1990) Low-temperature conformational transition within the [zinc-cytochrome c peroxidase, cytochrome c] electron-transfer complex. Journal Of The American Chemical Society, 112 (4) 1623-1625 doi:10.1021/ja00160a049
Roussel, M. F., Shurtleff, S. A., Downing, J. R., Sherr, C. J. (1990) A point mutation at tyrosine-809 in the human colony-stimulating factor 1 receptor impairs mitogenesis without abrogating tyrosine kinase activity, association with phosphatidylinositol 3-kinase, or induction of c-fos and junB genes. Proceedings of the National Academy of Sciences, 87 (17) 6738-6742 doi:10.1073/pnas.87.17.6738
 
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