Matches in SemOpenAlex for { <https://semopenalex.org/work/W3177344478> ?p ?o ?g. }
- W3177344478 endingPage "214071" @default.
- W3177344478 startingPage "214071" @default.
- W3177344478 abstract "Splitting the reduction potential of electron transport (ET) proteins and redox metalloenzymes into the enthalpic and entropic contributions is an insightful practice to gaining insight into the molecular determinants of the thermodynamic propensity of the metal center to accept or release electrons. The strict control of such propensity is essential for the functioning of the electron transport chains in bioenergetics and the organized network of the countless reactions of the redox metabolism in all organisms. Here, the first comprehensive overview is offered on the thermodynamic data obtained in the last three decades for the main classes of ET species, namely c-type cytochromes and proteins containing T1 copper and iron-sulfur centers, along with some heme metalloenzymes. These families show many common features in the balance of the enthalpic and entropic terms, which will be brought to light. The enthalpic terms related to ligation features in the first coordination sphere of the metal and weak binding and electrostatics in the surrounding matrix do count a lot in this balance. Reduction entropy is much less important that it would appear from the raw thermodynamic data, particularly for electron transport (ET) metalloproteins. This is due to reduction-induced solvent-related molecular events which dominate the measured entropy changes but affect much less the reduction free energy due to the compensatory effects of the associated enthalpic terms (a phenomenology known as enthalpy-entropy compensation, EEC). Thus the entropy changes seldom exert a real influence on the E°′ of metalloredox proteins; this is restricted to metal sites subjected to reduction-induced protein-based changes in the accessible configurational microstates. It follows that in most cases, especially for ET species, the E° changes due to point mutations, ligand binding and charge changes have an ultimate enthalpic origin. Hence, they should be accounted for with coordination chemistry and electrostatics notions. Only if they don’t, protein-based entropic effects could play a role. In this review, we go through the data gathered for the main classes of ET species and heme enzymes that brought us to this conclusion." @default.
- W3177344478 created "2021-07-05" @default.
- W3177344478 creator A5023599155 @default.
- W3177344478 creator A5041825942 @default.
- W3177344478 creator A5050529895 @default.
- W3177344478 creator A5050951483 @default.
- W3177344478 creator A5068179321 @default.
- W3177344478 creator A5070580947 @default.
- W3177344478 date "2021-10-01" @default.
- W3177344478 modified "2023-10-18" @default.
- W3177344478 title "The enthalpic and entropic terms of the reduction potential of metalloproteins: Determinants and interplay" @default.
- W3177344478 cites W1013569042 @default.
- W3177344478 cites W10180145 @default.
- W3177344478 cites W1199177259 @default.
- W3177344478 cites W1210608600 @default.
- W3177344478 cites W140375574 @default.
- W3177344478 cites W1486879703 @default.
- W3177344478 cites W1492471113 @default.
- W3177344478 cites W1504066663 @default.
- W3177344478 cites W1505729327 @default.
- W3177344478 cites W1507782118 @default.
- W3177344478 cites W1511788070 @default.
- W3177344478 cites W1513634340 @default.
- W3177344478 cites W1517059941 @default.
- W3177344478 cites W1523829738 @default.
- W3177344478 cites W1530120986 @default.
- W3177344478 cites W1534403612 @default.
- W3177344478 cites W1552415157 @default.
- W3177344478 cites W1561104226 @default.
- W3177344478 cites W1579445302 @default.
- W3177344478 cites W1583540770 @default.
- W3177344478 cites W1589968476 @default.
- W3177344478 cites W1599140686 @default.
- W3177344478 cites W1605369876 @default.
- W3177344478 cites W1655200277 @default.
- W3177344478 cites W1673073738 @default.
- W3177344478 cites W1687791458 @default.
- W3177344478 cites W176368695 @default.
- W3177344478 cites W1849447163 @default.
- W3177344478 cites W193624147 @default.
- W3177344478 cites W1963540054 @default.
- W3177344478 cites W1963692701 @default.
- W3177344478 cites W1963740551 @default.
- W3177344478 cites W1963755747 @default.
- W3177344478 cites W1963953346 @default.
- W3177344478 cites W1963995993 @default.
- W3177344478 cites W1964430082 @default.
- W3177344478 cites W1964680892 @default.
- W3177344478 cites W1965059091 @default.
- W3177344478 cites W1965498221 @default.
- W3177344478 cites W1965532585 @default.
- W3177344478 cites W1966162026 @default.
- W3177344478 cites W1966664123 @default.
- W3177344478 cites W1966857278 @default.
- W3177344478 cites W1967011060 @default.
- W3177344478 cites W1967028169 @default.
- W3177344478 cites W1967997654 @default.
- W3177344478 cites W1968322640 @default.
- W3177344478 cites W1968474058 @default.
- W3177344478 cites W1968547522 @default.
- W3177344478 cites W1970504039 @default.
- W3177344478 cites W1970527001 @default.
- W3177344478 cites W1971500510 @default.
- W3177344478 cites W1971562886 @default.
- W3177344478 cites W1971943723 @default.
- W3177344478 cites W1972464599 @default.
- W3177344478 cites W1973316236 @default.
- W3177344478 cites W1973537942 @default.
- W3177344478 cites W1973630631 @default.
- W3177344478 cites W1974089886 @default.
- W3177344478 cites W1975048860 @default.
- W3177344478 cites W1975452827 @default.
- W3177344478 cites W1976173612 @default.
- W3177344478 cites W1977336508 @default.
- W3177344478 cites W1978965855 @default.
- W3177344478 cites W1979121246 @default.
- W3177344478 cites W1979225897 @default.
- W3177344478 cites W1979331948 @default.
- W3177344478 cites W1979841825 @default.
- W3177344478 cites W1979879775 @default.
- W3177344478 cites W1980065294 @default.
- W3177344478 cites W1980480161 @default.
- W3177344478 cites W1980911985 @default.
- W3177344478 cites W1981385100 @default.
- W3177344478 cites W1981521205 @default.
- W3177344478 cites W1982343040 @default.
- W3177344478 cites W1982945266 @default.
- W3177344478 cites W1983658492 @default.
- W3177344478 cites W1983783982 @default.
- W3177344478 cites W1984701855 @default.
- W3177344478 cites W1984933445 @default.
- W3177344478 cites W1985309676 @default.
- W3177344478 cites W1985975492 @default.
- W3177344478 cites W1986879027 @default.
- W3177344478 cites W1987220178 @default.
- W3177344478 cites W1988018208 @default.
- W3177344478 cites W1988151159 @default.
- W3177344478 cites W1988458932 @default.