Nature of O2 and CO binding to metalloporphyrins and heme proteins.
نویسندگان
چکیده
منابع مشابه
Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection against reactive oxygen species. Despite the diverse structures and functions of these proteins, they share common mechanistic grounds. An open-shell transition metal like iron or copper is employed to interact with O2 and its derived intermedi...
متن کاملA comparative study of O2, CO and CN binding to heme IX protein models.
Parametrization of a molecular-mechanics program to include terms specific for five- and six-coordinate transition metal complexes results in computer-simulated structures of heme complexes. The principal new feature peculiar to five and six coordination is a term that measures the effect of electron-pair repulsion modified by the ligand electronegativity and takes into account the different st...
متن کاملBinding and Docking Interactions of NO, CO and O2 in Heme Proteins as Probed by Density Functional Theory
Dynamics and reactivity in heme proteins include direct and indirect interactions of the ligands/substrates like CO, NO and O(2) with the environment. Direct electrostatic interactions result from amino acid side chains in the inner cavities and/or metal coordination in the active site, whereas indirect interactions result by ligands in the same coordination sphere. Interactions play a crucial ...
متن کاملLigand Binding to Heme Proteins
The 02, CO, and alkyl isocyanide-binding properties of a variety of vertebrate and invertebrate heme proteins have been compared in detail to those of protoheme mOn0-3-( 1-imidazoy1)-propylamide monomethyl ester in aqueous suspensions of soap micelles. The proteins examined include: cytochrome P-450,,, from Pseudomonasputida, beef heart cytochrome c oxidase, yeast cytochrome c peroxidase, a and...
متن کاملBinding of O2 and CO to hemes and hemoproteins.
Enthalpies and entropies have been determined for the reversible binding of O2 and CO to chelated protoheme, a compound having a covalently attached imidazole bound to the iron. The values, based upon 1 atm standard state, are delta HO2 = -14.0 kcal (1 kcal = 4.18 kJ)/mol, delta SO2 = -35 eu, delta HCO = -17.5 kcal/mol, delta SCO = -34 eu, delta H identical to O2 = 21 kcal/mol (dissociation), a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1976
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.73.10.3333