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Literature DB >> 21625690

Peroxidase activity enhancement of horse cytochrome c by dimerization.

Zhonghua Wang¹, Takashi Matsuo, Satoshi Nagao, Shun Hirota.

Abstract

The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin π-cation radical) species were detected in the reactions with hydrogen peroxide and meta-chloroperbenzoic acid, respectively. These results show that oligomeric cytochrome c can contribute as a proapoptotic conformer by the increased peroxidase activity.

Entities: Chemical Gene Species

Mesh：

Substances：
Cytochromes c

Year: 2011 PMID： 21625690 DOI： 10.1039/c1ob05552f

Source DB: PubMed Journal: Org Biomol Chem ISSN： 1477-0520 Impact factor: 3.876

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Cited

21 in total

1. Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c.

Authors: Simanta Sarani Paul; Pallabi Sil; Shubhasis Haldar; Samaresh Mitra; Krishnananda Chattopadhyay
Journal: J Biol Chem Date: 2015-04-14 Impact factor: 5.157

2. Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity.

Authors: Haotian Lei; Bruce E Bowler
Journal: J Phys Chem B Date: 2019-10-14 Impact factor: 2.991

3. Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping.

Authors: Masaru Yamanaka; Satoshi Nagao; Hirofumi Komori; Yoshiki Higuchi; Shun Hirota
Journal: Protein Sci Date: 2015-01-14 Impact factor: 6.725

4. Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.

Authors: Masaru Yamanaka; Makoto Hoshizumi; Satoshi Nagao; Ryoko Nakayama; Naoki Shibata; Yoshiki Higuchi; Shun Hirota
Journal: Protein Sci Date: 2017-02-14 Impact factor: 6.725

5. A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.

Authors: Jeanine F Amacher; Fangfang Zhong; George P Lisi; Michael Q Zhu; Stephanie L Alden; Kevin R Hoke; Dean R Madden; Ekaterina V Pletneva
Journal: J Am Chem Soc Date: 2015-06-24 Impact factor: 15.419

Peroxidase activity enhancement of horse cytochrome c by dimerization.

1. Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c.

2. Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity.

3. Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping.

4. Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.

5. A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.

6. Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity.

7. The Human Cytochrome c Domain-Swapped Dimer Facilitates Tight Regulation of Intrinsic Apoptosis.

Review 8. Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions.

9. Effect of methionine80 heme coordination on domain swapping of cytochrome c.

10. Interaction of dimeric horse cytochrome c with cyanide ion.