Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 15 May 1992:
Vol. 256. no. 5059, pp. 1007 - 1009
DOI: 10.1126/science.256.5059.1007

Articles

Electron-Tunneling Pathways in Cytochrome c

Deborah S. Wuttke 1, Morten J. Bjerrum 1, Jay R. Winkler 1, and Harry B. Gray 1

1 Beckman Institute, California Institute of Technology, Pasadena, CA 91125

Distant Fe2+-Ru3+ electronic couplings have been extracted from intramolecular electrontransfer rates in Ru(histidinex) (where X = 33, 39, 62, and 72) derivatives of cytochrome c. The couplings increase according to 62 (0.0060) < 72 (0.057) < 33 (0.097) < 39 (0.11 per wave numbers); however, this order is out of line with the histidine to heme edge-edge distances [62 (14.8) > 39 (12.3) > 33 (11.1) > 72 (8.4 angstroms)]. The rates (and the couplings) correlate with the lengths of sgr-tunneling pathways comprised of covalent bonds, hydrogen bonds, and through-space jumps from the histidines to the heme group. Space jumps greatly decrease couplings: One from Pro71 to Met80 extends the sgr-tunneling length of the His72 pathway by roughly 10 covalent-bond units.

Submitted on December 27, 1991
Accepted on March 10, 1992


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Effects of interface mutations on association modes and electron-transfer rates between proteins.
S. A. Kang and B. R. Crane (2005)
PNAS 102, 15465-15470
   Abstract »    Full Text »    PDF »
Electron Tunneling Through Organic Molecules in Frozen Glasses.
O. S. Wenger, B. S. Leigh, R. M. Villahermosa, H. B. Gray, and J. R. Winkler (2005)
Science 307, 99-102
   Abstract »    Full Text »    PDF »
Definition of the Interaction Domain for Cytochrome c on Cytochrome c Oxidase. II. RAPID KINETIC ANALYSIS OF ELECTRON TRANSFER FROM CYTOCHROME c TO RHODOBACTER SPHAEROIDES CYTOCHROME OXIDASE SURFACE MUTANTS.
K. Wang, Y. Zhen, R. Sadoski, S. Grinnell, L. Geren, S. Ferguson-Miller, B. Durham, and F. Millett (1999)
J. Biol. Chem. 274, 38042-38050
   Abstract »    Full Text »    PDF »
Evidence That MgATP Accelerates Primary Electron Transfer in a Clostridium pasteurianum Fe Protein-Azotobacter vinelandii MoFe Protein Nitrogenase Tight Complex.
J. M. Chan, M. J. Ryle, and L. C. Seefeldt (1999)
J. Biol. Chem. 274, 17593-17598
   Abstract »    Full Text »    PDF »
Direct evaluation of electronic coupling mediated by hydrogen bonds: implications for biological electron transfer.
P. de Rege, S. Williams, and M. Therien (1995)
Science 269, 1409-1413
   Abstract »    PDF »
Electron tunneling in proteins: coupling through a beta strand.
R Langen, I. Chang, J. Germanas, J. Richards, Winkler JR, and H. Gray (1995)
Science 268, 1733-1735
   Abstract »    PDF »
Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase.
L. M. Geren, J. R. Beasley, B. R. Fine, A. J. Saunders, S. Hibdon, G. J. Pielak, B. Durham, and F. Millett (1995)
J. Biol. Chem. 270, 2466-2472
   Abstract »    Full Text »    PDF »
Effective coupling in biological electron transfer: exponential or complex distance dependence?.
J. Evenson and M Karplus (1993)
Science 262, 1247-1249
   Abstract »    PDF »
Electron-tunneling pathways in proteins.
D. Beratan, J. Onuchic, Winkler JR, and H. Gray (1992)
Science 258, 1740-1741
   PDF »
Structural models for the metal centers in the nitrogenase molybdenum-iron protein.
J Kim and D. Rees (1992)
Science 257, 1677-1682
   Abstract »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)