Optical Rotatory Dispersion of Oxidized and Reduced Cytochrome c<sup>*</sup>

Ulmer, David D.

doi:10.1021/bi00881a017

Cited by 58 publications

(29 citation statements)

References 30 publications

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“…The value of optical rotatory dispersion (115,116) in determining whether a protein has a high, moderate, or low a-helical content has been confirmed. Estimates of the a-helix contents of myoglobin (117,118), lysozyme (119), ribonuclease (120), chymotrypsin (121), carboxypeptidase A (122), carbonic anhydrase (123), and cytochrome c (124) are in qualitative accord with the crystallographic results. The use of fluorescence spectroscopy in measuring the polarity of the environment of tryptophan residues in protein (125) has been confirmed.…”

Section: Stryersupporting

confidence: 56%

Implications of X-Ray Crystallographic Studies of Protein Structure

Stryer¹

1968

Annu. Rev. Biochem.

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Section: Stryersupporting

confidence: 56%

Implications of X-Ray Crystallographic Studies of Protein Structure

Stryer¹

1968

Annu. Rev. Biochem.

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“…The reduced form of horse heart cytochrome c was prepared by adding an excess of sodium ascorbate to reduce the oxidized version, followed by dialysis to remove the excess ascorbate. 65 Briefly, 60 μg of the oxidized cytochrome c was dissolved in 1.5 mL of 0.01 M potassium phosphate buffer (pH 7.0), and mixed with 1.5 mL of 0.1 M sodium ascorbate in 0.01 M potassium phosphate buffer (pH 7.0). The mixture was stirred for 1 hour at 4 °C and the resulting solution was transferred into Slide-A-Lyzer dialysis cassette (Thermo Scientific, Rochford, IL, USA) using a syringe and then dialyzed against 0.01M phosphate buffer (pH 7.0).…”

Section: Methodsmentioning

confidence: 99%

Use of Metal Oxide Nanoparticle Band Gap To Develop a Predictive Paradigm for Oxidative Stress and Acute Pulmonary Inflammation

Zhang¹,

Ji²,

Xia³

et al. 2012

ACS Nano

759

865

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We demonstrate for 24 metal oxide (MOx) nanoparticles that it is possible to use conduction band energy levels to delineate their toxicological potential at cellular and whole animal levels. Among the materials, the overlap of conduction band energy (Ec) levels with the cellular redox potential (−4.12 to −4.84 eV) was strongly correlated to the ability of Co3O4, Cr2O3, Ni2O3, Mn2O3 and CoO nanoparticles to induce oxygen radicals, oxidative stress and inflammation. This outcome is premised on permissible electron transfers from the biological redox couples that maintain the cellular redox equilibrium to the conduction band of the semiconductor particles. Both single parameter cytotoxic as well as multi-parameter oxidative stress assays in cells showed excellent correlation to the generation of acute neutrophilic inflammation and cytokine responses in the lungs of CB57 Bl/6 mice. Co3O4, Ni2O3, Mn2O3 and CoO nanoparticles could also oxidize cytochrome c as a representative redox couple involved in redox homeostasis. While CuO and ZnO generated oxidative stress and acute pulmonary inflammation that is not predicted by Ec levels, the adverse biological effects of these materials could be explained by their solubility, as demonstrated by ICP-MS analysis. Taken together, these results demonstrate, for the first time, that it is possible to predict the toxicity of a large series of MOx nanoparticles in the lung premised on semiconductor properties and an integrated in vitro/in vivo hazard ranking model premised on oxidative stress. This establishes a robust platform for modeling of MOx structure-activity relationships based on band gap energy levels and particle dissolution. This predictive toxicological paradigm is also of considerable importance for regulatory decision-making about this important class of engineered nanomaterials.

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“…Changes in oxidation state, medium, and ligand, and modifications of amino acid residues were reflected in differences in ORD (351,(357)(358)(359)(360)(361)(362) and magneto optical rotatory dispersion spectra (363)(364)(365)(366). Implication tyrosine and tryptophan residues in oxidation-reduction dependent and other conformational changes resulted from ORD (358,360) and other (367) studies.…”

Section: Cytochrome ¢mentioning

confidence: 99%

Porphyrin Proteins and Enzymes

Caughey¹

1967

Annu. Rev. Biochem.

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In 1942 Theorell (1) published a paper on the magnetic properties of crystalline horseradish peroxidase and some of its derivatives, in which he stated, These determinations are to be regarded as a stage in our attempts to throw some light on the general problem: What conditions the great differences in the effects of the hemin ferments, despite their apparent uniformity in the composition hemin plus protein? Since in all cases the fermentative reactions take place at the iron atom or atoms, one imagines that the way in which the iron atoms are built into the molecule is of decisive importance for their mode of functioning .... We must of course also take into account an interaction between the iron atom and more re mote groups in the protein part. This interaction must, however, be weak in rela tion to the effect of the groups in the protein part that are directly coupled to the iron atom. Our first task is thus to try to ascertain the way in which the hemin is bound to the protein part. But not even if this proves successful can one count on getting a full insight into the way a hemin ferment takes effect.In discussing his now classic information about effects of ligand differences on magnetic susceptibilities Theorell continued, Now that sufficient experience of the magnetic properties of the proto-hemin proteides has been gained, it is possible to establish ... rules regarding the relation between the spectrum and the way the iron is bound.He listed the spectral characteristics of the four classes of compounds known at that time: (a) ferric compounds with essentially ionic bonds; (b) ferric compounds with essentially covalent bonds: (c) ferrous compounds with essentially ionic bonds; and (d) ferrous compounds with essentially covalent bonds. He added the reservation that groups (b) and (d) cannot be unambiguously distinguished by absorption spectrum only. Conventional wisdom today modifies Theorell's classification by the use of the terms high-spin and low-spin for ionic and covalent, respectively, but the same problems posed in 1942 by Theorell-the relationships between structure, 1 The survey of literature pertaining to this review was concluded in October 1966 .2 Myoglobin and hemoglobin denote iron (II) forms, in preference to the terms deoxymyoglobin and deoxyhemoglobin. Metmyoglobin and methemoglobin denote the "acid" iron (III) forms; other derivatives will be clearly designated.

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Optical Rotatory Dispersion of Oxidized and Reduced Cytochrome c^*

Cited by 58 publications

References 30 publications

Implications of X-Ray Crystallographic Studies of Protein Structure

Implications of X-Ray Crystallographic Studies of Protein Structure

Use of Metal Oxide Nanoparticle Band Gap To Develop a Predictive Paradigm for Oxidative Stress and Acute Pulmonary Inflammation

Porphyrin Proteins and Enzymes

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Optical Rotatory Dispersion of Oxidized and Reduced Cytochrome c*

Cited by 58 publications

References 30 publications

Implications of X-Ray Crystallographic Studies of Protein Structure

Implications of X-Ray Crystallographic Studies of Protein Structure

Use of Metal Oxide Nanoparticle Band Gap To Develop a Predictive Paradigm for Oxidative Stress and Acute Pulmonary Inflammation

Porphyrin Proteins and Enzymes

Contact Info

Product

Resources

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Optical Rotatory Dispersion of Oxidized and Reduced Cytochrome c^*