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Cofactor

Figure Bl.15.16. Two-pulse ESE signal intensity of the chemically reduced ubiqumone-10 cofactor in photosynthetic bacterial reaction centres at 115 K. MW frequency is 95.1 GHz. One dimension is the magnetic field value Bq, the other dimension is the pulse separation x. The echo decay fiinction is anisotropic with respect to the spectral position. Figure Bl.15.16. Two-pulse ESE signal intensity of the chemically reduced ubiqumone-10 cofactor in photosynthetic bacterial reaction centres at 115 K. MW frequency is 95.1 GHz. One dimension is the magnetic field value Bq, the other dimension is the pulse separation x. The echo decay fiinction is anisotropic with respect to the spectral position.
A substantial fraction of the named enzymes are oxido-reductases, responsible for shuttling electrons along metabolic pathways that reduce carbon dioxide to sugar (in the case of plants), or reduce oxygen to water (in the case of mammals). The oxido-reductases that drive these processes involve a small set of redox active cofactors , that is, small chemical groups that gain or lose electrons. These cofactors include iron porjDhyrins, iron-sulfur clusters and copper complexes as well as organic species that are ET active. [Pg.2974]

The transpose of a square matrix is, of course, another square matrix. The transpose of a symmetric matrix is itself. One particularly important transpose matrix is the adjoint natris, adJA, which is the transpose matrix of cofactors. For example, the matrix of cofactors ul liie 3x3 matrix... [Pg.35]

In thi.-. case the adjoint matrix is the same as the matrix of cofactors (as A is a symmetric. njlri.x). The inverse of a matrix is obtained by dividing the elements of the adjoint matrix tlie determinant ... [Pg.35]

Metabolic Functions. Chromium (ITT) potentiates the action of insulin and may be considered a cofactor for insulin (137,138). In in vitro tests of epididymal fat tissue of chromium-deficient rats, Cr(III) increases the uptake of glucose only in the presence of insulin (137). The interaction of Cr(III) and insulin also is demonstrated by experimental results indicating an effect of Cr(III) in translocation of sugars into ceUs at the first step of sugar metaboHsm. Chromium is thought to form a complex with insulin and insulin receptors (136). [Pg.387]

Adenosine. Adenosine [58-61-7] (Ado), (29), a purine nucleoside, is an intracellular constituent acting as both an enzyme cofactor... [Pg.523]

In addition, Ee protein-1 has at least two noncatalytic roles related to nitrogen fixation, and presumably Ee protein-2 and Ee protein-3 do also. The first function is somehow involved in the early stages of EeMo-cofactor biosynthesis because mutant strains having a deletion in nifil produce neither Ee protein nor EeMo-cofactor, rather only a EeMo-cofactor-deficient apo-MoEe protein (104,105). The second role involves insertion of preformed EeMo-cofactor into these apo-MoEe proteins (106). [Pg.87]

The VFe protein also has the equivalent of P-cluster pairs which have similar properties to those found in the MoFe protein (159). No information is available on whether P-cluster pairs exist in the FeFe protein, but because of the relatively high sequence identity and the similar genetic basis of its biosynthesis, the occurrence seems highly likely. The catalytic role assigned to the P-cluster pair involves accepting electrons from the Fe protein for storage and future deUvery to the substrate via the FeMo-cofactor centers. As of this writing (ca early 1995), this role has yet to be proved. [Pg.89]

Fig. 7. View of the FeMo-cofactor prosthetic group of the nitrogenase MoFe protein with some of the surrounding amino acid residues where ( ) represents the molybdenum coordinated to a-His-442 and homocitrate (at the top), ( ) represents the iron, interspersed with the sulfur (O) and carbon... Fig. 7. View of the FeMo-cofactor prosthetic group of the nitrogenase MoFe protein with some of the surrounding amino acid residues where ( ) represents the molybdenum coordinated to a-His-442 and homocitrate (at the top), ( ) represents the iron, interspersed with the sulfur (O) and carbon...
Although FeMo-cofactor is clearly knpHcated in substrate reduction cataly2ed by the Mo-nitrogenase, efforts to reduce substrates using the isolated FeMo-cofactor have been mosdy equivocal. Thus the FeMo-cofactor s polypeptide environment must play a critical role in substrate binding and reduction. Also, the different spectroscopic features of protein-bound vs isolated FeMo-cofactor clearly indicate a role for the polypeptide in electronically fine-tuning the substrate-reduction site. Site-directed amino acid substitution studies have been used to probe the possible effects of FeMo-cofactor s polypeptide environment on substrate reduction (163—169). Catalytic and spectroscopic consequences of such substitutions should provide information concerning the specific functions of individual amino acids located within the FeMo-cofactor environment (95,122,149). [Pg.90]

HammerheadRtbozyme. A small RNA molecule that catalyzes cleavage of the phosphodiester backbone of RNA is known as the hammerhead ribozyme. This ribozyme occurs namrally in certain vimses where it facihtates a site-specific self-cleavage at the phosphate and generates a 2 3 -cychc phosphate and a 5 -hydroxyl terminus. The reaction requires a divalent metal ion, such as or, as a cofactor. Whereas the... [Pg.256]

Gofactors. Frequendy proteins exist in their native state in association with other nonprotein molecules or cofactors, which are cmcial to their function. These may be simple metal ions, such as Fe " in hemerythrin or Ca " in calmodulin a heme group, as for the globins nucleotides, as for dehydrogenases, etc. [Pg.211]

In the EHE process, a starch slurry is prepared and calcium, as the chloride or hydroxide, is added as a cofactor to provide heat stabiUty to the enzyme. The starch slurry is passed through a stream injection heater and held at temperature for about one hour. The resulting 4—8 DE hydrolyzate is then subjected to a heat treatment in a hoi ding tube, redosed with enzyme, and allowed to react for one hour to a DE level of 10—15. [Pg.290]

HES is produced from 93—96% dextrose hydrolyzate that has been clarified, carbon-treated, ion-exchanged, and evaporated to 40—50% dry basis. Magnesium is added at a level of 0.5—5 mAf as a cofactor to maintain isomerase stabiUty and to prevent enzyme inhibition by trace amounts of residual calcium. The feed may also be deaerated or treated with sodium bisulfite at a level of 1—2-mAf SO2 to prevent oxidation of the enzyme and a resulting loss in activity. [Pg.294]

Vitamins aie specific organic compounds that are essential for normal metabolism. Many participate as cofactors or coen2ymes ia mammalian biochemical reactions. The common thread for the diverse chemical stmctures of the vitamins is that they ate micronutrients. Micronutrients are compounds that are requited ia only small amounts and are not synthesized by humans, either at all or, at least, ia sufficient quantity for metaboHc needs. Vitamins are obtained from the diet or as synthetic preparations used ia food fortification or supplements. [Pg.3]


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0-Glucosidase, cofactors

1.2- Dithiolenes cofactor biosynthesis

ATPase cofactors

Aconitase cofactors

Activator-recruited cofactor

Aldehyde oxidoreductase molybdenum cofactor structure

Amino acid dehydrogenase cofactor regeneration

Amino acid racemases cofactors

Amino cofactor-independent

Analytical reagents cofactors

Antibodies cofactor catalysis

Antithrombin III heparin cofactor

Apoenzyme-cofactor interactions

Applications in Redox Cofactor Electrochemistry

Artificial cofactor regenerating enzymes

Ascorbic acid cofactors

Availability of Cosubstrates and Cofactors

B-12 cofactor

Binding sites, introduction cofactors

Biocatalysis cofactor recycling

Biocatalyst cofactor regeneration

Biocatalyst enzyme-coupled cofactor

Biocatalyst substrate-coupled cofactor

Biogenesis of TPQ and Related Cofactors

Biological systems activity cofactor

Biomimetic cofactors

Biopterin cofactors

Bioreduction cofactor regeneration

Biosynthesis, dithiolene cofactor

Biotin protein cofactor

Biotin sulfoxide reductase molybdenum cofactor

Blood clotting cofactors

Blood coagulation thrombin-cofactor interactions

Caspase Cofactor

Catalytic antibodies cofactor catalysis

Chemiluminescence cofactors

Cobalamin cofactor

Cobalamin cofactor synthase

Cobalamin, methyl cofactor

Cobalamine cofactors

Coenzymes and Cofactors

Cofactor Engineering for Xylitol Production in Recombinant Saccharomyces cerevisiae

Cofactor F-430

Cofactor FeMoCo

Cofactor M reductase

Cofactor M reductase molecular weight

Cofactor NAD H

Cofactor NADH

Cofactor Recycle in Multi-Step Oxidizing Biocatalytic Systems

Cofactor Regeneration in Whole-Cells

Cofactor Substitution In Vitro

Cofactor acetylene reduction

Cofactor binding

Cofactor clusters

Cofactor coenzyme

Cofactor consumption

Cofactor containing biomolecules

Cofactor corrins

Cofactor cyanide binding

Cofactor depletion

Cofactor dissociation

Cofactor engineering

Cofactor immobilization

Cofactor incorporation

Cofactor interaction screening

Cofactor iron-sulfur

Cofactor ligation

Cofactor of an element

Cofactor optical sensor

Cofactor organic solvents

Cofactor protein-integrated

Cofactor proton binding

Cofactor pyridoxal phosphate

Cofactor reconstitution

Cofactor reconstitution approach

Cofactor recycling

Cofactor recycling systems

Cofactor recycling, biocatalytic

Cofactor recycling, biocatalytic asymmetric reduction

Cofactor regeneration

Cofactor regeneration systems

Cofactor regeneration systems reactions

Cofactor regeneration systems, for

Cofactor regeneration, chemical

Cofactor requirements

Cofactor requirements, microsomal enzymes

Cofactor specificity

Cofactor substitution

Cofactor supplementation, treatment

Cofactor thiol binding

Cofactor topaquinone

Cofactor, acetylation

Cofactor, acetylation fatty acid oxidation

Cofactor-Independent with Activated Substrates

Cofactor-dependent enzyme

Cofactor-enzyme affinity complexes

Cofactor-labeled antigens

Cofactors Competition

Cofactors Concanavalin

Cofactors biocatalytic reactions

Cofactors classification

Cofactors commonly encountered

Cofactors dinucleotide

Cofactors electrochemical regeneration

Cofactors fixed

Cofactors for catalysis

Cofactors for enzymatic reactions

Cofactors in catalysis

Cofactors metal/organic

Cofactors of Caspase Activation

Cofactors of glucose oxidase

Cofactors porphyrins 212

Cofactors primitive 203

Cofactors reduction

Cofactors structure

Cofactors transition metals

Cofactors with PSII

Cofactors, Coenzymes, and Prosthetic Groups

Cofactors, fluorescent

Cofactors, inorganic

Cofactors, introduction

Complement cofactor

Complex flavin cofactor

Copper cofactor

Copper cofactor biogenesis

Copper enzyme cofactor

Cosubstrates and cofactors

Cytochrome bci Metal Cofactor Specifics

Cytochrome cofactor regenerating enzymes

Degradation flavin cofactor

Dehydrogenases cofactor

Dehydrogenases, Changing Cofactor Specificity

Dermatan sulfate cofactor activation

Determinant cofactor

Dihydronicotinamide cofactors

Diiron cofactor

Dopamine hydroxylase cofactor

Effective Cofactor Recycling

Electrochemical cofactor recycling

Electron transfer cofactors

Enzyme cofactor

Enzyme cofactor binding, implication

Enzyme cofactors calcium

Enzyme-bound cofactor regeneration

Enzymes cofactor regeneration

Enzymes cofactor specificity

Enzymes cofactors for

FAD cofactor

Fe-Mo cofactor

FeMo cofactor, FeMoco

FeMo-cofactor

FeMo-cofactor resting states

FeMo-cofactor structure

FeMo-cofactor substrate binding

Flavin adenine dinucleotide FAD)-cofactor

Flavin adenine dinucleotide cofactor

Flavin cofactors

Flavin mononucleotide cofactor

Flavins cofactor function

Fluorescent Enzyme Cofactors

Folic acid cofactors

Fucosylation with Integrated Cofactor Regeneration

Fusion cofactors

Galactose oxidase cofactor biogenesis

Galactose oxidase tyrosine-cysteine cofactor

Galactosylation with Galactosyltransferases and Integrated Cofactor Regeneration

Glycogen phosphorylase metabolism cofactor

Heat shock protein cofactors

Heme cofactor

Heme groups cofactors specific enzymes

Heme proteins with cofactors

Heparin cofactor

Heparin cofactor II

Heterocyclic cofactors

Hsp70 and Its Cofactors

Hydride-transfer reactions involving nicotinamide cofactors

In cofactor regeneration

In oxidation-reduction cofactor

In situ cofactor recycling

Inorganic cofactors, hemes

Introduction cofactor requirements

Iron-molybdenum cofactor

Iron-molybdenum cofactor composition

Iron-molybdenum cofactor, FeMoco

Iron-molybdenum cofactor, FeMoco electron reduction

Iron-molybdenum cofactor, FeMoco structure

Iron-molybdenum cofactor, FeMoco synthesis

Iron-sulfur clusters FeMo-cofactor

Iron-sulfur clusters FeMoco-cofactor

Isobacteriochlorin cofactor

L-0-Lysine mutase cofactor requirements

Magnesium cofactor

Magnesium enzyme cofactor

Magnesium, as cofactor

Matrices and Cofactors

Matrix cofactor

Matrix of cofactors

Membrane cofactor protein

Membrane cofactor protein (MCP

Metabolic engineering cofactor

Metabolic transformations cofactors

Metal Cofactor Specifics

Metal cofactor interactions

Metal cofactors

Metal cofactors, introduction

Metal cofactors, polypeptide-bound

Metal ion cofactors

Metal-binding cofactors

Metalloporphyrins cofactor

Metals as cofactors

Methyltransferases cofactors

Minerals cofactors

MoFe-cofactor

Modeling the Azadithiolate Cofactor

Molybdenum cofactor (Moco

Molybdenum cofactor biosynthesis

Molybdenum cofactor domain

Molybdenum cofactor model systems

Molybdenum cofactor nitrogenase complexes

Molybdenum cofactor proposed structure

Molybdenum cofactor reduced form

Molybdenum cofactor structure

Molybdenum cofactor sulfurase

Molybdenum cofactor synthesis

Molybdenum cofactors 208

Molybdenum enzymes cofactors

Molybdenum iron protein cofactor

Molybdenum iron protein cofactor structure

Molybdopterin cofactor

NADH cofactor regeneration

NADH cofactor, recycling

NADH/NADPH cofactors

NADH/NADPH cofactors enzymes

NADP cofactor

Natural product enzyme cofactors

Nickel cofactors

Nicotinamide adenine dinucleotide cofactor

Nicotinamide adenine dinucleotide hydride reduced form cofactor

Nicotinamide adenine dinucleotide phosphate cofactors

Nicotinamide cofactor

Nicotinamide cofactors NAD

Nitrogenase MoFe protein cofactor

Nitrogenase cofactor

Nitrogenase cofactor, FeMoco

Nitrogenase molybdenum, cofactor

Nitrogenase molybdenum-iron protein FeMo-cofactor

Nitrogenase, iron-molybdenum cofactor

Nuclear receptor-cofactor complexes

Nuclear receptor-cofactor inhibitors

Nuclear receptor-cofactor interaction

Nucleic acid polymerase cofactors

Nucleoside cofactors

Organic cofactor

Other Coenzymes and Cofactors

Other Cofactors

Oxidation-reduction cofactors

Oxidoreductase cofactor immobilization

Oxygen evolution inorganic cofactors

PLP cofactor binding

PPAR cofactors

Pantetheine cofactors

Peroxidases cofactor regeneration

Phenylalanine hydroxylase cofactor

Phosphorylases cofactor

Photoisomerizable FAD cofactor

Photoisomerization cofactor

Photosynthetic bacteria cofactor arrangement

Photosynthetic reaction center electron transfer cofactors

Positive cofactor

Potassium cofactor

Preparation and Reactions of the FeMo Cofactor Model Clusters

Prochiral ketones with cofactor

Prosthetic Groups, Cofactors, and Post-Translational Modifications

Prosthetic Groups, and Cofactors

Prosthetic group or cofactor

Proteins cofactors

Proteins metal cofactors

Proteus mirabilis molybdenum cofactor

Pterin cofactor

Pyridoxal phosphate as a cofactor

Pyridoxal phosphate, coenzyme cofactor

Pyridoxamine cofactor

Pyruvate dehydrogenase cofactors

Quinone cofactors

Radical cofactors

Reaction center cofactors

Recycling of Cofactors

Redox active cofactors

Redox cofactors

Redox cofactors imbalance

Reduction cofactor recycling

Regeneration of dihydronicotinamide cofactors

Regeneration of the cofactor NADH

Relay-cofactor

Releasing the Spring Cofactor- and Substrate-assisted Activation of Factor IXa

Reorganization energy cofactors

Ribonucleotide reductase tyrosyl radical cofactor

Ribozymes, cofactors

Ristocetin cofactor activity

S cofactors

Saturation of Tryptophan Dioxygenase with Its Heme Cofactor

Selenium cofactors

Specificity and cofactors

Spectroscopic studies molybdenum cofactor

Spectroscopy pterin cofactors

Stoichiometric cofactors

Strategies for Cofactor Regeneration in Biocatalyzed Reductions

Substrate-coupled cofactor

Sulfite oxidase molybdenum cofactor

Synthesis with cofactor regeneration

TTQ cofactor

Targeting the Nuclear Receptor-Cofactor Interaction

Tetrahydropteridine cofactor

Tetrahydropterin cofactor

The Active Site of Nitrogenase FeMo-Cofactor

The FeMo-Cofactor

The Molybdenum Cofactor (Mo-co)

The Roles of Cofactors

The Tetrapyrrolic Cofactors

Thiamine enzyme cofactor

Transport molybdenum cofactor

Tungsten cofactor

Vitamin cofactor functions

Vitamin cofactor, labeling

Vitamins cofactor forms

Xanthine oxidase molybdenum cofactor

Xenobiotic Receptor Cofactors and Coregulators

Xylitol cofactor engineering

Yeast, tubulin cofactors

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