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2 edition of Contribution of protein environment to redox potentials of rubredoxin and cytochrome c found in the catalog.

Contribution of protein environment to redox potentials of rubredoxin and cytochrome c

Vaishali S. Shenoy

Contribution of protein environment to redox potentials of rubredoxin and cytochrome c

by Vaishali S. Shenoy

  • 162 Want to read
  • 16 Currently reading

Published .
Written in English

    Subjects:
  • Cytochrome.,
  • Proteins -- Physiological transport.

  • Edition Notes

    Statementby Vaishali S. Shenoy.
    The Physical Object
    Paginationx, 82 p. :
    Number of Pages82
    ID Numbers
    Open LibraryOL16952100M

    Understanding Rubredoxin Redox Potentials: Role of H-Bonds on Model Complexes Ana Patricia Gámiz-Hernández, Artur S. Galstyan and Ernst-Walter Knapp Journal of Chemical Theory and Computation 5 (10), Cited by: In Chapter 4, the role of the second-sphere protein environment in tuning E0 is elucidated for T1 Cu sites. The reduction potentials of T1 Cu sites in proteins and enzymes with identical first coordination spheres around the redox active Cu can vary by ~ mV.

    The book provides an up-to-date review of the bioinorganic chemistry of this metal and its ions; it covers the biogeochemistry of lead, its use (not only as gasoline additive) and anthropogenic release into the environment, its cycling and speciation in the atmosphere, in waters, soils, and sediments, and also in mammalian organs. Mitochondrial flow of electrons from NADH to oxygen, cytochrome C, Cytochrome C oxidase. Metalloenzymes: Structure and reactivity- Zinc enzymes: carboxypeptidase, carbonic anhydrase, alcoholdehydrogenase. Cu enzyme: superoxide dismutase. Mo enzyme: Xanthine oxidase, nitrate reductase. Fe enzymes: catalase, peroxidise and cytochrome P

    Protein Name PDB - ID Binding Energy (kcal/mol) Antigen 85C 1dqz Cytochrome P Crystal structure of 3-bromopyruvate modified isocitrate lyase (icl) 1f8m EmbR 2ff4 Hydroxymycolate synthase MmaA4 2fk7 - Zinc-substituted rubredoxin B 2kn Cell. Protein Name PDB - ID Binding Energy (kcal/mol) Antigen 85C 1dqz Cytochrome P Crystal structure of 3-bromopyruvate modified isocitrate lyase (icl) 1f8m EmbR 2ff4 Hydroxymycolate synthase MmaA4 2fk7 - Zinc-substituted rubredoxin B 2kn Cell: 2ko


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Contribution of protein environment to redox potentials of rubredoxin and cytochrome c by Vaishali S. Shenoy Download PDF EPUB FB2

This multisubunit protein transfers electrons from cytochrome c to O 2. Two of the protein components of complex IV are cytochromes a and a 3. This complex is unique in the ETC in having copper as a component. However, copper is a common component in other oxidase enzymes that also react with O 2.

Vaishali S. Shenoy has written: 'Contribution of protein environment to redox potentials of rubredoxin and cytochrome c' -- subject(s): Physiological transport, Proteins, Cytochrome Asked in Biology.

Vaishali S. Shenoy has written: 'Contribution of protein environment to redox potentials of rubredoxin and cytochrome c' -- subject(s): Physiological transport, Proteins, Cytochrome Asked in. Rubredoxin. Rubredoxins are small electron transfer proteins.

Rubredoxin from Pyrococcus furiosus is composed of 53 amino acid residues for nearly 6 kDa in mass. Electron transfer is handled by a single Fe redox center coordinated to four cysteinyl thiolates.

These large variations in redox potentials of ISC models and ISC in Rd are due to specific conformational symmetries adopted by the ligands due to both the protein environment and type and the. In cytochrome c, the coordination of the axial Met Sδ atom to the heme Fe atom occurs in one of two distinctly different stereochemical manners, i.e., R and S configurations, depending upon which.

Zdravko Bradic, Patricia C. Harrington and Ralph G. Wilkins, Reduction of methemerythrin by deoxymyoglobin: a protein-protein redox reaction not involving electron-transfer proteins, Biochemistry, 18, 5, (), ().Cited by: 3. X-ray absorption spectroscopy at the sulfur K-edge at ∼ eV has been applied to a series of mononuclear iron−sulfur complexes to determine the covalency and its distribution over the ligand field split d-orbitals.

A comparison is made between the S K-edges of a model and three different rubredoxin proteins to define the changes in covalency upon incorporation of the site into the by: In particular, tuning the redox potential (E M) of the FeS center is critical for controlling the conditions under which the protein responds to its environment and its interacting partners.

As a class, FeS proteins span a wide redox range (1) under normal cellular conditions, indicating that FeS centers are fundamentally by: All life on Earth is dependent on biologically mediated electron transfer (i.e., redox) reactions that are far from thermodynamic equilibrium.

Biological redox reactions originally evolved in prokaryotes and ultimately, over the first ∼ billion years of Earth's history, formed a global electronic circuit.

To maintain the circuit on a global scale requires that oxidants and reductants be Cited by: an important contribution to the understanding of biochemical systems.

Cell Biochemistry and Function "Lippard and Berg's book should be very useful at academic institutions offering coursework in bioinorganic chemistry.

Their style of writing and the book's format are perfect for that audience." Science and Technology (Chemistry). Iron (/ ˈ aɪ ər n /) is a chemical element with symbol Fe (from Latin: ferrum) and atomic number It is a metal that belongs to the first transition series and group 8 of the periodic table.

It is by mass the most common element on Earth, forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust.

Iron, 26 Fe Iron Appearance lustrous Group: group 8. Because of the biologically accessible metal-centered reduction potential and the ability to reach four oxidation states in vivo (+2, + 3, + 4, and + 5), cationic Mn porphyrins can redox cycle with a number of biologic molecules, such as cellular reductants, flavoenzymes and cytochrome P reductase, and can mimic the cyt P family of Cited by: NMR and visible spectroscopy coupled to redox measurements were used to determine the equilibrium thermodynamic properties of the four haems in cytochrome c3 under conditions in which the protein was bound to ligands, the small anion phosphate and the protein rubredoxin with the iron in the active site replaced by zinc.

Mixed quantum-classical (quantum mechanical/molecular mechanical (QM/MM)) simulations have strongly contributed to providing insights into the understanding of several structural and mechanistic aspects of biological molecules.

They played a particularly important role in metal binding proteins, where the electronic effects of transition metals have to be explicitly taken into account for the Cited by: Publications Theses.

Undergraduate Honors Thesis, Carleton College,“Sulfato and Oxalatochromium (III) Complexes” Ph.D. Thesis, Harvard University,“Proton Magnetic Resonance Studies of the Structure and Binding Sites of Staphylococcal Nuclease” Book Review. A natural bond orbital (NBO) analysis of unpaired electron spin density in metalloproteins is presented, which allows a fast and robust calculation of paramagnetic NMR parameters.

Approximately 90% of the unpaired electron spin density occupies metal–ligand NBOs, allowing the majority of the density to be modeled by only a few NBOs that reflect the chemical bonding by: "Beginning with an overview of metals and selected nonmetals in biology, the book supports the interdisciplinary nature of this vibrant area of research by providing an introduction to basic coordination chemistry for biologists and structural and molecular biology for chemists.

Comprehensive Coordination Chemistry II (CCC II) is the sequel to what has become a classic in the field, Comprehensive Coordination Chemistry, published in CCC II builds on the first and surveys new developments authoritatively in over newly comissioned chapters, with an emphasis on current trends in biology, materials science and.

Oxalate:ferredoxin oxidoreductase (OOR) is an unusual member of the thiamine pyrophosphate (TPP)-dependent 2-oxoacid:ferredoxin oxidoreductase (OFOR) family in that it catalyzes the coenzyme A (CoA)-independent conversion of oxalate into 2 equivalents of carbon dioxide.

This reaction is surprising because binding of CoA to the acyl-TPP intermediate of other OFORs results in formation of a CoA Cited by: 3. In contrast, cytochrome c has a redox potential of volts.

A wide range of redox potentials for iron is achieved in biology by subtle differences in protein structure, as listed in Table Notice the large difference in the potential of cytochrome c and rubredoxin (Figure ), volts vs.

.Antioxidant potency. The ability to catalyze O 2 ˙ − dismutation (log k cat in Table I) best describes the antioxidant potency of the cationic Mn(III) N-alkylpyridylporphyrins [1,2].The reason lies in the fact that the SOD-like activity parallels the ONOO − scavenging ability and, in turn, the ability of MnPs to finely tune cellular redox-based transcriptional activity [1,2,12,14].Cited by: Cytochrome P cam and Other Bacterial P Enzymes.

Authors; Authors and affiliations; and Goldkorn, T.,The contribution of electrostatic factors to the oxidation—reduction potentials of c-type cytochromes, in: Electron Transport andControl of heure protein redox potential. Linear free energy relationship between Cited by: