Proton titration curve of yeast iso-1-ferricytochrome c. Electrostatic and conformational effects of point mutations.

PubWeight™: 0.76‹?›

🔗 View Article (PMID 1848095)

Published in Biochemistry on March 05, 1991

Authors

P D Barker1, M R Mauk, A G Mauk

Author Affiliations

1: Department of Biochemistry, University of British Columbia, Vancouver, Canada.

Articles by these authors

Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5. Biochemistry (1993) 2.14

Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry (1998) 2.01

Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72 trimethylation. J Biol Chem (2000) 1.50

Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature (1985) 1.41

Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis. Biochemistry (1991) 1.37

Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Eng (1989) 1.35

Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase. Biochemistry (1999) 1.29

Transmutation of a heme protein. Proc Natl Acad Sci U S A (1993) 1.25

A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket. Biochim Biophys Acta (1997) 1.25

Stability of lipid vesicles in tissues of the mouse: a gamma-ray perturbed angular correlation study. Proc Natl Acad Sci U S A (1979) 1.22

Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry (2000) 1.19

Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: electrostatic properties of the high- and low-affinity cytochrome binding sites on the peroxidase. Biochemistry (1994) 1.12

Dissociation of heme from myoglobin and cytochrome b5: comparison of behavior in solution and the gas phase. Biochemistry (1997) 1.09

Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium. Biochemistry (1989) 1.08

Preparation of lipid vesicles containing high levels of entrapped radioactive cations. Anal Biochem (1979) 1.04

The peroxidase activity of a hemin--DNA oligonucleotide complex: free radical damage to specific guanine bases of the DNA. J Am Chem Soc (2001) 1.04

Spectrophotometric analysis of the interaction between cytochrome b5 and cytochrome c. Biochemistry (1982) 1.02

Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7. Biochemistry (1990) 1.01

Targeting of lipid vesicles: specificity of carbohydrate receptor analogues for leukocytes in mice. Proc Natl Acad Sci U S A (1980) 1.01

Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry (1993) 1.00

Vesicle targeting: timed release and specificity for leukocytes in mice by subcutaneous injection. Science (1980) 0.99

Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry (1991) 0.98

Mutation-induced perturbation of the cytochrome c alkaline transition. Biochemistry (1989) 0.97

Recombinant human erythrocyte cytochrome b5. Biochemistry (1994) 0.97

Fate of lipid vesicles in vivo: a gamma-ray perturbed angular correlation study. Proc Natl Acad Sci U S A (1977) 0.97

The proximal ligand variant His93Tyr of horse heart myoglobin. Biochemistry (1995) 0.96

Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c. Biochemistry (1990) 0.96

Monooxygenase activity of cytochrome c peroxidase. J Biol Chem (1992) 0.96

Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant. Biochem J (1998) 0.95

Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential. Biochemistry (2001) 0.94

Crosslinking of cytochrome c and cytochrome b5 with a water-soluble carbodiimide. Reaction conditions, product analysis and critique of the technique. Eur J Biochem (1989) 0.93

The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. Eur J Biochem (1999) 0.92

Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5. Biochemistry (1997) 0.91

N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J (1998) 0.91

Responses of two protein-protein complexes to solvent stress: does water play a role at the interface? Biophys J (1993) 0.90

Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity. Biochemistry (1996) 0.90

The peroxide complex of yeast cytochrome c peroxidase contains two distinct radical species, neither of which resides at methionine 172 or tryptophan 51. J Biol Chem (1987) 0.90

Models for the complexes formed between cytochrome b5 and the subunits of methemoglobin. J Biol Chem (1983) 0.90

Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. FEBS Lett (1996) 0.90

Sulfmyoglobin. Resonance Raman spectroscopic evidence for an iron-chlorin prosthetic group. J Biol Chem (1984) 0.90

In vitro evolution of horse heart myoglobin to increase peroxidase activity. Proc Natl Acad Sci U S A (1998) 0.90

Cytochrome c peroxidase-cytochrome c complex: locating the second binding domain on cytochrome c peroxidase with site-directed mutagenesis. Biochemistry (2000) 0.89

Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie (1994) 0.89

Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin. Biochemistry (1995) 0.89

Reaction of human myoglobin and H2O2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical. J Biol Chem (2001) 0.88

Electrostatic modification of the active site of myoglobin: characterization of the proximal Ser92Asp variant. Biochemistry (1996) 0.87

Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5. J Bioenerg Biomembr (1995) 0.86

Thermodynamic cycles as probes of structure in unfolded proteins. Biochemistry (1996) 0.86

NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex. Science (1990) 0.85

Reaction of human myoglobin and H2O2. Involvement of a thiyl radical produced at cysteine 110. J Biol Chem (2000) 0.85

Chain amino termini of the cat hemoglobins and the response to 2,3-diphosphoglycerate and adenosine triphosphate. J Biol Chem (1971) 0.85

Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants. Biochemistry (1995) 0.85

Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization. Biochemistry (1994) 0.85

Three-dimensional structure of cyanomet-sulfmyoglobin C. Proc Natl Acad Sci U S A (1994) 0.85

Photooxidation of the protoporphyrin-apomyoglobin complex. Biochemistry (1973) 0.84

pH, electrolyte, and substrate-linked variation in active site structure of the Trp51Ala variant of cytochrome c peroxidase. Biochemistry (1995) 0.84

Interaction between cytochrome b5 and human methemoglobin. Biochemistry (1982) 0.83

Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proc Natl Acad Sci U S A (1987) 0.83

Electrostatic analysis of the interaction of cytochrome c with native and dimethyl ester heme substituted cytochrome b5. Biochemistry (1986) 0.83

Proton linkage of complex formation between cytochrome c and cytochrome b5: electrostatic consequences of protein-protein interactions. Biochemistry (1991) 0.83

Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry. Biochemistry (1997) 0.83

Site-directed mutations at phenylalanine-190 of manganese peroxidase: effects on stability, function, and coordination. Biochemistry (1997) 0.83

FTIR analysis of the interaction of azide with horse heart myoglobin variants. Biochemistry (1994) 0.82

Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c. Biochemistry (2000) 0.82

Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (s) nitrosation dependence on the absence or presence of oxygen. J Biol Chem (2000) 0.82

Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase. J Biol Chem (1991) 0.82

A cytochrome c variant resistant to heme degradation by hydrogen peroxide. Chem Biol (2000) 0.82

Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex. Biochemistry (1993) 0.81

Analysis of the kinetics of electron transfer reactions of hemoglobin and myoglobin with inorganic complexes. Biochem Biophys Res Commun (1979) 0.81

Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase. Biochemistry (1993) 0.81

The protoporphyrin-apoperoxidase complex. Photooxidation studies. Biochemistry (1974) 0.80

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli. FEBS Lett (1994) 0.80

Structural changes in cytochrome c upon hydrogen-deuterium exchange. Biochemistry (1993) 0.80

Kinetics of hemoprotein reduction and interprotein heme transfer. Biochemistry (1985) 0.80

Crystallization and preliminary diffraction data for horse heart metmyoglobin. J Mol Biol (1987) 0.80

Reaction of human myoglobin and peroxynitrite: characterizing biomarkers for myoglobin-derived oxidative stress. Biochem Biophys Res Commun (2001) 0.79

Spectroscopic and functional studies of a novel quadruple myoglobin variant with increased peroxidase activity. J Inorg Biochem (1998) 0.79

Effects of organic phosphates on oxygen equilibria and kinetics of -SH reaction in feline hemoglobins. Arch Biochem Biophys (1972) 0.79

Structural characterization of heme ligation in the His64-->Tyr variant of myoglobin. J Biol Chem (1994) 0.79

pH-linked binding of Mn(II) to manganese peroxidase. Biochemistry (1998) 0.79

Charge reversal of a critical active-site residue of cytochrome-c peroxidase: characterization of the Arg48-->Glu variant. Eur J Biochem (1997) 0.79

Kinetic analysis of metsulphmyoglobin and metmyoglobin reduction by Fe(EDTA)2-. Biochem J (1985) 0.78

A DNA oligonucleotide-hemin complex cleaves t-butyl hydroperoxide through a homolytic mechanism. Inorg Chem (2001) 0.77

Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. FEBS Lett (1991) 0.77

Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis. Proc Natl Acad Sci U S A (1986) 0.77

Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein. Biochim Biophys Acta (1999) 0.77

Spectroscopic, electrochemical, and ligand binding properties of the horse heart metmyoglobin His64-Tyr variant. Biochim Biophys Acta (1994) 0.77

Hemin is kinetically trapped in cytochrome b(5) from rat outer mitochondrial membrane. Biochem Biophys Res Commun (2000) 0.77

Nitrosylhemoglobin Wood: effects of inositol hexaphosphate on thiol reactivity and electron paramagnetic resonance spectrum. Biochemistry (1975) 0.76

Functional comparison of specifically cross-linked hemoglobins biased toward the R and T states. Biophys J (1998) 0.76

NMR study of the interaction between cytochrome b5 and cytochrome c. Observation of a ternary complex formed by the two proteins and [Cr(en)3]3+. FEBS Lett (1987) 0.76