Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Heme protein

4 Heme proteins. - Rivera and Caignan have reviewed recent research involving NMR of paramagnetic hemes and heme proteins. [Pg.577]

Bertini et report a detailed study of the magnetic properties of myglobin, in which they determined the axial and orthorhombic terms of the paramagnetic susceptibility tensor using a combination of hyperfine chemical shift measurements and static suscetibility measurements (Evans Method). The determination of the magnetic anisotropy provided a measurement of the residual dipolar couplings and also permitted a separation of the contact and pseudocontact chemical shift contributions of resonances of the Fe(III) ligands. [Pg.577]

Du et have determined the magnitude and orientation of the paramagnetic susceptibility tensor of the cyanomet complex of an 02-avid hemoglobin from the trematode Paramphistomum epiclitum. They used proton hyperfine chemical shifts and paramagnetic relaxation enhancements to probe the chemical bonding at the metal center. [Pg.577]

Ma et alP have analysed the pseudocontact chemical shifts of high-spin, ferrous heme in deoxy myoglobin from Aplysia limacinato determine the orientation and magnetic anisotropy of the heme prosthetic group within the heme pocket. This knowledge allowed a separation of contact and pseudocontact contributions to the chemical shifts of the heme resonances, and, from these, a mapping of spin density on the heme. [Pg.577]

Vu et al. have carried out a detailed analysis of H, and N hyperfine chemical shifts in two cyanobacterial hemoglobins. This study focuses on the the properties of an unusual cross-link between one of the heme vinyl groups and a histidine located in the C-terminal helix. [Pg.577]


Plenary 7 7. P M Champion et al, e-mail address champ neu.edu (TRRRS). Femtosecond impulsive preparation and timing of ground and excited state Raman coherences in heme proteins. Discovery of coherence transfer along a de-ligation coordinate. See above for fiirther connnent. [Pg.1219]

Champion P M, Rosea F, Chang W, Kumar A, Christian J and Demidov A 1998 Femtosecond coherence spectroscopy of heme proteins XVith int. Conf on Raman Spectroscopy ed A M Heyns (New York Wley) pp 73-6... [Pg.1227]

Zhu L, Li P, Huang M, Sage J T and Champion P M 1994 Real time observation of low frequency heme protein vibrations using femtosecond coherence spectroscopy Phys. Rev. Lett. 72 301-4... [Pg.1998]

Zhu L, Wang W, Sage J T and Champion P M 1995 Femtosecond time-resolved vibrational spectroscopy of heme proteins J. Raman Spectrosc. 26 527-34... [Pg.1998]

Lian T, Locke B, Kholodenko Y and Hochstrasser R M 1994 Energy flow from solute to solvent probed by femtosecond IR spectroscopy malachite green and heme protein solutions J. Rhys. [Pg.1999]

Hill J R ef a/1996 Ultrafast infrared speotrosoopy in biomoleoules aotive site dynamios of heme proteins Biospectroscopy 2 277-99... [Pg.3051]

Lingle R J, Xu X, Zhu H, Yu S-C and Hopkins J B 1991 Piooseoond Raman study of energy flow in a photoexoited heme protein J. Phys. Chem. 95 9320-31... [Pg.3051]

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. [Pg.306]

DA Case, M Karplus. Dynamics of ligand binding to heme proteins. 1 Mol Biol 132 343-368, 1979. [Pg.412]

Mossbauer spectroscopy in heme proteins. A. Trautwein, Struct. Bonding (Berlin), 1974, 20, 101-167 (115). [Pg.42]

Figure 5.14 Electrospray spectrum of holocytochrome c". Reprinted from Biochim. Bio-phys. Acta, 1412, Klarskov, K., Leys, D., Backers, K., Costa, H. S., Santos, H., Guisez, Y. and Van Beeumen, 1. 1., Cytochrome c" from the obligate methylotroph Methy-lophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides", 47-55, Copyright (1999), with permission from Elsevier Science. Figure 5.14 Electrospray spectrum of holocytochrome c". Reprinted from Biochim. Bio-phys. Acta, 1412, Klarskov, K., Leys, D., Backers, K., Costa, H. S., Santos, H., Guisez, Y. and Van Beeumen, 1. 1., Cytochrome c" from the obligate methylotroph Methy-lophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides", 47-55, Copyright (1999), with permission from Elsevier Science.
Tofield BC (1975) The Study of Covalency by Magnetic Neutron Scattering. 21 1-87 Trautwein AX, Bill E, Bominaar EL, Winkler H (1991) Iron-Containing Proteins and Related Analogs-Complementary Mossbauer, EPR and Magnetic Susceptibility Studies. 78 1-96 Trautwein AX (1974) Mossbauer-Spectroscopy on Heme Proteins. 20 101-167 Tressaud A, Dance J-M (1982) Relationships Between Structure and Low-Dimensional Magnetism in Fluorides. 52 87-146... [Pg.256]

Isocyanides [RNC] (174, 175) are isoelectronic with CO and have been extensively used as CO analogs in studies of heme proteins (176-180). W-Butyl isocyanide (N-BIC) behaves as a CO analog at both the CODH and ACS active sites (181). N-BIC competes with CO in the CO oxidation reaction, is a sluggish reductant, and causes EPR spectral changes at Clusters A, B, and C similar to those elicited by CO. [Pg.320]

Proteins may be classified on the basis of the solubility, shape, or function or of the presence of a prosthetic group such as heme. Proteins perform complex physical and catalytic functions by positioning specific chemical groups in a precise three-dimensional arrangement that is both functionally efficient and physically strong. [Pg.39]

It is estimated that 1 g of hemoglobin yields 35 mg of bihmbin. The daily bihmbin formation in human adults is approximately 250-350 mg, deriving mainly from hemoglobin but also from ineffective erythro-poiesis and from various other heme proteins such as cytochrome P450. [Pg.278]

There is now sufficient information in the literature to conclude that nitrite reacts with the non-heme proteins of meat. [Pg.296]

Methylanaline could be transnitrosated with nitrite and S-nitrosocysteine and also by a simulated protein bound nitrite. In the latter case, an important factor was the local concentration of nitrosothiol groups on the matrix. The effects of S-nitrosocysteine as an inhibitor of lipid oxidation, as a color developer, and as an anticlostridial, have been reported recently in a turkey product (31). The Molar concentration of RSNO equating to 25 ppm nitrite gave similar results for color and inhibition of lipid oxidation but had less anti-clostridial activity. Transnitrosation between RSNO and heme protein was demonstrated. [Pg.296]


See other pages where Heme protein is mentioned: [Pg.541]    [Pg.199]    [Pg.211]    [Pg.146]    [Pg.146]    [Pg.324]    [Pg.125]    [Pg.138]    [Pg.218]    [Pg.219]    [Pg.221]    [Pg.222]    [Pg.7]    [Pg.146]    [Pg.165]    [Pg.40]    [Pg.278]    [Pg.572]    [Pg.328]    [Pg.289]    [Pg.294]    [Pg.296]    [Pg.289]    [Pg.368]    [Pg.196]    [Pg.130]   
See also in sourсe #XX -- [ Pg.270 , Pg.271 ]

See also in sourсe #XX -- [ Pg.532 ]

See also in sourсe #XX -- [ Pg.171 ]

See also in sourсe #XX -- [ Pg.546 ]

See also in sourсe #XX -- [ Pg.452 , Pg.457 ]

See also in sourсe #XX -- [ Pg.2 ]

See also in sourсe #XX -- [ Pg.843 , Pg.844 , Pg.1058 ]

See also in sourсe #XX -- [ Pg.452 , Pg.457 ]

See also in sourсe #XX -- [ Pg.57 , Pg.58 , Pg.68 , Pg.69 , Pg.82 , Pg.149 , Pg.150 , Pg.151 , Pg.152 , Pg.153 , Pg.154 , Pg.155 , Pg.156 , Pg.157 , Pg.158 , Pg.159 , Pg.160 , Pg.164 , Pg.167 , Pg.168 , Pg.268 , Pg.269 , Pg.280 , Pg.295 , Pg.298 , Pg.309 ]

See also in sourсe #XX -- [ Pg.262 ]

See also in sourсe #XX -- [ Pg.843 , Pg.844 ]

See also in sourсe #XX -- [ Pg.69 , Pg.70 , Pg.77 , Pg.87 ]

See also in sourсe #XX -- [ Pg.276 , Pg.299 ]

See also in sourсe #XX -- [ Pg.120 , Pg.121 , Pg.122 , Pg.123 , Pg.124 ]

See also in sourсe #XX -- [ Pg.137 ]

See also in sourсe #XX -- [ Pg.253 ]

See also in sourсe #XX -- [ Pg.868 ]

See also in sourсe #XX -- [ Pg.843 , Pg.844 , Pg.1058 ]

See also in sourсe #XX -- [ Pg.843 , Pg.844 ]

See also in sourсe #XX -- [ Pg.416 ]

See also in sourсe #XX -- [ Pg.4 , Pg.262 ]

See also in sourсe #XX -- [ Pg.546 ]

See also in sourсe #XX -- [ Pg.44 , Pg.45 ]

See also in sourсe #XX -- [ Pg.37 ]

See also in sourсe #XX -- [ Pg.36 ]

See also in sourсe #XX -- [ Pg.546 ]

See also in sourсe #XX -- [ Pg.40 , Pg.42 ]

See also in sourсe #XX -- [ Pg.315 ]

See also in sourсe #XX -- [ Pg.236 ]

See also in sourсe #XX -- [ Pg.6 , Pg.34 ]

See also in sourсe #XX -- [ Pg.349 ]




SEARCH



Amino acids heme protein maquette

Cytochrome P450 heme-containing proteins

Cytochrome heme-protein linkage

De novo design heme proteins

Electron transport heme proteins

Engineering heme proteins

Ferric Forms of Heme Proteins

Heme Oxygenase Is a Stress Protein

Heme Oxygenase The Protein

Heme group proteins

Heme groups flavin proteins

Heme oxygenase stress protein

Heme protein as oxygen sensor

Heme protein mimics

Heme protein models

Heme protein, cytochrome

Heme protein, cytochrome biotransformation

Heme protein, cytochrome reductive metabolism

Heme proteins Hemerythrin

Heme proteins Soret region

Heme proteins azide binding

Heme proteins carbon monoxide binding

Heme proteins catalase

Heme proteins chloroperoxidase

Heme proteins conformation

Heme proteins dioxygen reactivity

Heme proteins direct evolution

Heme proteins distance measurements

Heme proteins electrochemistry

Heme proteins ferric forms

Heme proteins flavocytochrome

Heme proteins forms

Heme proteins from myeloperoxidase

Heme proteins functionalization

Heme proteins green hemes

Heme proteins hemichromes

Heme proteins hemoglobin

Heme proteins high spin forms

Heme proteins horseradish peroxidase

Heme proteins iron active site

Heme proteins kinetics

Heme proteins leghemoglobin

Heme proteins lipid oxidation initiation

Heme proteins marker bands

Heme proteins methemoglobin

Heme proteins model complexes

Heme proteins myeloperoxidase

Heme proteins myoglobin

Heme proteins myoglobin reconstitution

Heme proteins paramagnetic

Heme proteins peptide systems

Heme proteins possible origin

Heme proteins protein scaffolds

Heme proteins proton coupled electron transfer

Heme proteins reactions

Heme proteins reactions with hydrogen peroxid

Heme proteins reactions with oxygen

Heme proteins reconstitutional modification

Heme proteins resonance Raman spectra

Heme proteins resonance Raman spectroscopy

Heme proteins spectroscopic characterization

Heme proteins structure-function relationship

Heme proteins with cofactors

Heme proteins, Mossbauer spectroscop

Heme proteins, catalytic properties

Heme proteins, enzymes

Heme proteins, major

Heme proteins, modification

Heme proteins, roles

Heme-based proteins

Heme-containing proteins

Heme-iron proteins

Heme-protein crosslinking

Heme-protein fold

Heme-protein-hemopexin

Heme-reconstituted de novo protein

Heme-thiolate proteins

Hemoglobin heme protein linkage

Hemopexin heme-protein interactions

High-Spin NO Complexes with Non-Heme Iron Proteins

High-spin ferric forms of heme proteins

Induced Circular Dichroism of Heme and Chlorophyll Bound to Proteins

Iron, cytochrome heme protein

Linked functions heme proteins

Magnetic susceptibility, heme protein complexes

Measurements in Heme Proteins

Metal-substituted heme protein

Mononuclear non-heme iron proteins

NADPH heme proteins

Non-Heme Iron-Containing Proteins

Non-heme iron proteins

Non-heme proteins

Novo Heme Proteins

Organic Reactions Catalyzed by Heme Proteins

Other Modes of P450 Heme Degradation and Protein Denaturation

Oxygen binding by heme proteins

Oxygen binding of, to heme proteins

Oxygen heme proteins

Oxygen-binding heme protein

P450 Protein by Heme Fragments

Peroxidases heme iron-containing proteins

Porphyrin heme proteins

Proteins heme activator protein

Proteins heme, reaction with nitric oxide

Reaction of NO with Heme Proteins and Metals

Rhodospirillum rubrum heme protein

Simple Heme Protein Models

Spin Ferric Forms of Heme Proteins

Spin NO Complexes with Non-Heme Iron Proteins

© 2024 chempedia.info