The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications.
Willem H. Koppenol,E Margoliash +1 more
TLDR
This model describes quantitatively the relative activities of those CDNP-lysine cytochromes c which are modified outside of the interaction domain and it allows correction of the activities of Those modified inside the domain, on the front surface of the molecule, for the change in dipole moment.About:
This article is published in Journal of Biological Chemistry.The article was published on 1982-04-25 and is currently open access. It has received 345 citations till now. The article focuses on the topics: Cytochrome c peroxidase & Cytochrome c.read more
Citations
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Journal ArticleDOI
Electron transfers in chemistry and biology
Rudolph A. Marcus,Norman Sutin +1 more
TL;DR: In this paper, the electron transfer reactions between ions and molecules in solution have been the subject of considerable experimental study during the past three decades, including charge transfer, photoelectric emission spectra, chemiluminescent electron transfer, and electron transfer through frozen media.
Journal ArticleDOI
Classical Electrostatics in Biology and Chemistry
Barry Honig,Anthony Nicholls +1 more
TL;DR: A major revival in the use of classical electrostatics as an approach to the study of charged and polar molecules in aqueous solution has been made possible through the development of fast numerical and computational methods to solve the Poisson-Boltzmann equation for solute molecules that have complex shapes and charge distributions.
Journal ArticleDOI
Direct electrochemistry of redox proteins
Book ChapterDOI
Electrical Wiring of Redox Enzymes
TL;DR: In this paper, the functional electron transfer center of a redox enzyme can be electrically connected to an external source of current through a path of fast electron-relaying redox couples, achieved through electrostatically or covalently binding to the enzyme-proteins high molecular weight redox polycations having segments anchored to electrodes.
Journal ArticleDOI
The dielectric constant of a folded protein.
Michael K. Gilson,Barry Honig +1 more
TL;DR: A form of the Kirkwood–Fröhlich dielectric theory that applies to polar solids and folded proteins is developed, which incorporates a factor expressing the degree to which dipolar groups are constrained within the material's structure, as well as a generalized form of Kirkwood's correlation factor.
References
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Journal ArticleDOI
Alpha-helix dipole and properties of proteins
TL;DR: Phosphate moieties bind frequently at N-termini of helices in proteins and it is shown that this corresponds with an optimal interaction of the helix dipole and the charged phosphate.
Journal ArticleDOI
Ferricytochrome c: I. GENERAL FEATURES OF THE HORSE AND BONITO PROTEINS AT 2.8 A RESOLUTION
Richard E. Dickerson,Tsunehiro Takano,David Eisenberg,O.B. Kallai,Lalli Samson,Angela Cooper,Emanuel Margoliash +6 more
TL;DR: The structure of crystalline horse heart ferricytochrome c has been determined by x-ray methods to a resolution of 2.8 A, and the results have been extended to obtain the structure of bonito cy tochrome c as well.
Journal ArticleDOI
Effects of proteins on the thermotropic phase transitions of phospholipid membranes
TL;DR: A variety of proteins have been studied for their ability to interact and alter the thermotropic properties of phospholipid bilayer membranes as detected by differential scanning calorimeter, and it was concluded that in this case the protein was embedded within the bilayer, associating with a limited number of molecules via non-polar interactions, while the rest of the bilayers was largely unperturbed.
Journal ArticleDOI
Energetics of enzyme catalysis
TL;DR: Quantitative studies of the energetics of enzymatic reactions and the corresponding reactions in aqueous solutions indicate that charge stabilization is the most important energy contribution in enzyme catalysis.
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A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex.
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