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Iron protein proteins

W. A. Bulen, J. R. LeComte, R. C. Bums, and J. Hinkson, in A. San Pietro, ed., Non-Heme Iron Proteins Role in Lnerg Conversion Antioch Press, Yellow Springs, Ohio, 1965, p. 261. [Pg.95]

The lUBMB Commission on Nomenclature has issued a number of recommendations dealing with areas of a more biochemical nature (72), such as peptide hormones (86), conformation of polypeptide chains (87), abbreviations for nucleic acids and polynucleotides (88), iron—sulfur proteins (89), enzyme units (90), etc. The Commission has also produced rules and recommendations for naming enzymes (91,92). [Pg.120]

G Backes, Y Mino, TM Loehr, TE Meyer, MA Cusanovich, WV Sweeny, ET Adman, J Sand-ers-Loehr. The environment of Ee4S4 clusters in ferredoxms and high-potential iron proteins. New information from X-ray crystallography and resonance Raman spectroscopy. J Am Chem Soc 113 2055-2064, 1991. [Pg.411]

PJ Stephens, DR Jollie, A Warshel. Protein control of redox potentials of iron-sulfur proteins. Chem Rev 96 2491-2513, 1996. [Pg.412]

PD Swartz, T Ichiye. Protein contributions to redox potentials of iron-sulfur proteins An energy minimization study. Biophys J 73 2733-2741, 1997. [Pg.413]

PD Swartz, BW Beck, T Ichiye. Stiaictural origins of redox potential m iron-sulfur proteins Electrostatic potentials of crystal structures. Biophys 1 71 2958-2969, 1996. [Pg.414]

Nonrepetitive but well-defined structures of this type form many important features of enzyme active sites. In some cases, a particular arrangement of coil structure providing a specific type of functional site recurs in several functionally related proteins. The peptide loop that binds iron-sulfur clusters in both ferredoxin and high potential iron protein is one example. Another is the central loop portion of the E—F hand structure that binds a calcium ion in several calcium-binding proteins, including calmodulin, carp parvalbumin, troponin C, and the intestinal calcium-binding protein. This loop, shown in Figure 6.26, connects two short a-helices. The calcium ion nestles into the pocket formed by this structure. [Pg.182]

Wachtershanser has also suggested that early metabolic processes first occurred on the surface of pyrite and other related mineral materials. The iron-sulfur chemistry that prevailed on these mineral surfaces may have influenced the evolution of the iron-sulfur proteins that control and catalyze many reactions in modern pathways (including the succinate dehydrogenase and aconitase reactions of the TCA cycle). [Pg.664]

All these intermediates except for cytochrome c are membrane-associated (either in the mitochondrial inner membrane of eukaryotes or in the plasma membrane of prokaryotes). All three types of proteins involved in this chain— flavoproteins, cytochromes, and iron-sulfur proteins—possess electron-transferring prosthetic groups. [Pg.680]

Three protein complexes have been isolated, including the flavoprotein (FP), iron-sulfur protein (IP), and hydrophobic protein (HP). FP contains three peptides (of mass 51, 24, and 10 kD) and bound FMN and has 2 Fe-S centers (a 2Fe-2S center and a 4Fe-4S center). IP contains six peptides and at least 3 Fe-S centers. HP contains at least seven peptides and one Fe-S center. [Pg.683]

Table 25.8 Reduction potentials of some iron proteins... Table 25.8 Reduction potentials of some iron proteins...
Figure 25.9 Some non-haem iron proteins (a) rubredoxin in which the single Fe is coordinated, almost tetra-hedrally, to 4 cysteine-sulfurs, (b) plant ferredoxin, [Fe2S2(S-Cys)4], (c) [Fe4S4(S-Cys)4] cube of bacterial ferredoxins. (This is in fact distorted, the Fe4 and S4 making up the two interpenetrating tetrahedra, of which the latter is larger than the former). Figure 25.9 Some non-haem iron proteins (a) rubredoxin in which the single Fe is coordinated, almost tetra-hedrally, to 4 cysteine-sulfurs, (b) plant ferredoxin, [Fe2S2(S-Cys)4], (c) [Fe4S4(S-Cys)4] cube of bacterial ferredoxins. (This is in fact distorted, the Fe4 and S4 making up the two interpenetrating tetrahedra, of which the latter is larger than the former).
Other non-haem proteins, distinct from the above iron-sulfur proteins are involved in the roles of iron transport and storage. Iron is absorbed as Fe" in the human duodenum and passes into the blood as the Fe protein, transferrin, The Fe is in a distorted octahedral environment consisting of 1 x N, 3x0 and a chelating carbonate ion which... [Pg.1103]

Biochemical aspects of Fe—S linkages in non-aqueous heme iron proteins with special reference to Andrenodoxin. T. Kimura, Struct. Bonding (Berlin), 1968, 5, 2-40 (72). [Pg.36]

Metal-polypeptide interactions the conformational state of iron proteins. M. Llinas. Struct. Bonding (Berlin), 1973, 17, 135-220 (320). [Pg.43]


See other pages where Iron protein proteins is mentioned: [Pg.1403]    [Pg.905]    [Pg.1403]    [Pg.905]    [Pg.174]    [Pg.2990]    [Pg.28]    [Pg.434]    [Pg.442]    [Pg.385]    [Pg.476]    [Pg.87]    [Pg.393]    [Pg.396]    [Pg.398]    [Pg.405]    [Pg.405]    [Pg.124]    [Pg.189]    [Pg.191]    [Pg.680]    [Pg.784]    [Pg.1079]    [Pg.1093]    [Pg.1098]    [Pg.1098]    [Pg.1101]    [Pg.1102]    [Pg.1102]    [Pg.1103]    [Pg.351]    [Pg.389]    [Pg.94]    [Pg.20]    [Pg.34]   


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4Fe:4S cluster, nitrogenase iron-protein Fe

Aconitase iron-response element-binding protein

Animal iron-binding proteins

Azotobacter molybdenum-iron protein

Bacteria iron-storage proteins

Bacterial-Type Iron-Sulfur Proteins

Binuclear iron-oxo proteins

Biological Functions of Iron-Containing Proteins

Centers of iron-sulfur proteins

Chloroplasts iron-sulfur proteins

Chromatium, iron protein from

Clusters high-potential iron proteins

Comparisons of dinuclear iron centers in ferritins and other proteins

Complex Rieske iron sulfur protein

Copper and iron proteins

Copper reductases iron proteins

Corrinoid iron-sulfur protein

Cysteine-Containing Oligopeptide Model Complexes of Iron-Sulfur Proteins

Cytochrome Rieske iron sulfur protein

Cytosolic iron regulatory protein

Electrochemistry of Iron-Sulfur Proteins

Electron Spin Resonance Caused by Iron Proteins

Electron relaxation times, iron-sulfur proteins

Electron transfer iron proteins

Electron transfer iron-sulfur proteins

Electron transport chain iron-sulfur proteins

Electron transport iron-containing proteins

Enzymes iron-sulfur proteins

Enzymes nickel-iron proteins

Enzymes nickel-iron-sulfur proteins

Eukaryotes anaerobic, iron-sulfur proteins

Eukaryotes iron-sulfur proteins

Ferritin, an iron-storage protein

Haem-iron proteins

Heme proteins iron active site

Heme-iron proteins

High-Spin NO Complexes with Non-Heme Iron Proteins

High-potential iron protein, resonance

High-potential iron proteins

High-potential iron proteins cluster stability

High-potential iron proteins derivatives

High-potential iron proteins function

High-potential iron proteins primary

High-potential iron proteins redox properties

High-potential iron proteins residues

High-potential iron proteins solvent accessibility

High-potential iron proteins structure

High-potential iron-sulfur protein

High-potential iron-sulfur protein HiPIP

High-potential iron-sulfur proteins HiPIPs)

Hyperfine shift, iron-sulfur proteins

Iron (also proteins

Iron Regulatory Protein-1 RNA-Binding Activity

Iron Regulatory Proteins 1 and

Iron binding proteins lactoferrin

Iron binding proteins transferrin

Iron copper proteins

Iron in proteins

Iron protein , serum

Iron protein active centers

Iron protein domain structure

Iron protein effect

Iron protein electron transfer reactions

Iron protein electron transport

Iron protein from transferrin, physiologic

Iron protein high-potential type

Iron protein immunity

Iron protein in nitrogenase

Iron protein involving

Iron protein microbial

Iron protein other biochemical reactions

Iron protein properties

Iron protein release

Iron protein release from transferrin

Iron protein reticulocytes

Iron protein solubility

Iron protein stress-response mechanism

Iron protein structure-function correlation

Iron protein supply

Iron protein tertiary structure

Iron protein transport

Iron protein uptake, siderophore-mediated

Iron proteins

Iron proteins nucleotides, interaction with

Iron proteins redox properties

Iron proteins self-oxidization

Iron proteins site-directed mutagenesis

Iron proteins spectroscopy

Iron proteins structure

Iron regulator 7 protein

Iron regulatory proteins (IRP-1 and

Iron response element binding protein

Iron responsive element-binding protein (

Iron storage and transport proteins

Iron storage proteins, ferrihydrite

Iron storage proteins, ferrihydrite mineralization

Iron succinyl-protein complex

Iron sulfur proteins, high potential, oxidized

Iron, cytochrome heme protein

Iron-Sulfur Proteins in Organisms Harboring Hydrogenosomes and Mitosomes

Iron-binding protein

Iron-containing proteins

Iron-containing proteins and enzymes

Iron-containing proteins hemoglobins

Iron-containing proteins mammalian transferrin

Iron-containing proteins mediator molecules

Iron-containing proteins myoglobins

Iron-containing proteins redox potentials

Iron-containing proteins transferrin)

Iron-nickel-sulfur proteins

Iron-oxo proteins

Iron-processing proteins

Iron-protein complex

Iron-protein interface

Iron-protein, nitrogenase properties

Iron-regulatory protein

Iron-response proteins

Iron-responsive element binding protein IRE-BP)

Iron-responsive protein (IRP

Iron-sulfur protein clusters

Iron-sulfur protein complex

Iron-sulfur protein properties

Iron-sulfur protein/cluster aconitase

Iron-sulfur proteins

Iron-sulfur proteins Mossbauer spectra

Iron-sulfur proteins NiFe hydrogenase

Iron-sulfur proteins Rieske-type

Iron-sulfur proteins aconitase

Iron-sulfur proteins adenosine 5 -phosphosulfate reductas

Iron-sulfur proteins aldehyde oxidoreductase

Iron-sulfur proteins background, XII

Iron-sulfur proteins categories

Iron-sulfur proteins centers)

Iron-sulfur proteins characterization

Iron-sulfur proteins conformational change

Iron-sulfur proteins cubane structure

Iron-sulfur proteins eight irons

Iron-sulfur proteins electron paramagnetic resonance

Iron-sulfur proteins ferredoxins

Iron-sulfur proteins formate dehydrogenase

Iron-sulfur proteins fumarate reductase

Iron-sulfur proteins functions

Iron-sulfur proteins high-potential, thiolate complexes

Iron-sulfur proteins hydrogenases

Iron-sulfur proteins identification

Iron-sulfur proteins in sulfate-reducing bacteria

Iron-sulfur proteins ligand

Iron-sulfur proteins model compounds

Iron-sulfur proteins model studies

Iron-sulfur proteins nitrate reductase

Iron-sulfur proteins nitric oxide complexes

Iron-sulfur proteins nitrogenases rubredoxins

Iron-sulfur proteins oriented systems

Iron-sulfur proteins oxidation states

Iron-sulfur proteins polypeptide folding

Iron-sulfur proteins protein environment

Iron-sulfur proteins pyruvate-ferredoxin oxidoreductase

Iron-sulfur proteins reduction potential

Iron-sulfur proteins resonance Raman spectra

Iron-sulfur proteins rubredoxin

Iron-sulfur proteins solution structure

Iron-sulfur proteins spectrum

Iron-sulfur proteins spin densities

Iron-sulfur proteins succinate dehydrogenase

Iron-sulfur proteins sulfite reductase

Iron-sulfur proteins valence delocalization

Iron-sulfur proteins with other prosthetic groups

Iron-sulfur proteins, Mossbauer

Iron-sulfur proteins, Mossbauer spectroscopy

Iron-sulfur proteins, in anaerobic

Iron-sulfur proteins, in anaerobic eukaryotes

Iron-sulfur proteins, valence

Iron-sulfur proteins, valence electrons

Iron-sulphur proteins

Iron-sulphur redox proteins

Iron-tyrosinate proteins

Iron—sulfur proteins crystallography

Iron—sulfur proteins electronic properties

Iron—sulfur proteins examples

Iron—sulfur proteins structures

Iron—sulfur proteins vibrational modes

Low-potential iron-sulfur proteins

Metalloproteins high-potential iron proteins

Molybdenum iron protein cofactor

Molybdenum iron protein cofactor structure

Molybdenum iron protein structure

Molybdenum nitrogenase iron proteins

Molybdenum-iron protein

Molybdenum-iron protein in nitrogenase

Molybdenum-iron protein, nitrogenase properties

Mononuclear non-heme iron proteins

NMR Spectra of Iron Sulfur Proteins

NMR Spectra of Iron Sulfur Proteins Ivano Bertini, Claudio Luchinat, and

Nickel-iron proteins, hydrogenase

Nitric Oxide Complexes of Iron-Sulfur Proteins

Nitric Oxide Complexes of Other Nonheme Iron Proteins

Nitric oxide complexes nonheme iron proteins

Nitrogen molybdenum iron protein

Nitrogenase iron-protein structure

Nitrogenase molybdenum-iron protein FeMo-cofactor

Nitrogenase molybdenum-iron protein structure

Nitrogenases iron proteins

Non-Heme Iron-Containing Proteins

Non-haem iron proteins

Non-heme iron proteins

Nonheme iron proteins

Nonheme oxygen-binding iron proteins

Nonheme-iron protein mechanisms

Nuclear relaxation rates, iron-sulfur proteins

Nucleotide binding proteins, iron protein

Other Iron-containing Proteins

Other Types of Iron-Containing Enzymes and Proteins

Oxidation-reduction reactions nonheme iron proteins

Peptococcus aerogenes iron protein from

Peroxidases heme iron-containing proteins

Photosystem I Reduces NADP by Way of Iron-Sulfur Proteins

Plant-Type Iron-Sulfur Proteins

Protein bond, iron

Protein iron responsive

Protein iron-storage

Protein which reversibly bind iron

Proteins iron and

Proteins with Iron-Sulfur Clusters

Rieske iron protein

Rieske iron protein movement

Rieske iron protein states

Rieske iron protein tether

Rieske iron sulfur protein

Simple and Complex Iron-Sulfur Proteins

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing Bacteria

Spectra of iron-sulfur proteins

Spin NO Complexes with Non-Heme Iron Proteins

Sulfate-reducing bacteria iron-sulfur proteins

The Iron-Sulfur Proteins

The small protein contains a unique iron-sulfur center

Thiolate complexes, iron-sulfur proteins

Tungsten-selenium-iron protein

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