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Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states.

<div class='caption-title'>Structure of the heme region of cyt c and the location of Pro71 in the structure (pdb code: 1YIC).</div>
<div class='caption-title'>UV-Visible absorption spectra of cyt c P71H variant in the oxidized (solid line) and reduced (dashed line) states.</div>
Figure 3
Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX
OpenAccess logo PLoS One 6 e27219 (2011)
Cited: 6 times
EuropePMC logo PMID: 22087268

Abstract

To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.

Articles - 2lir mentioned but not cited (1)

  1. Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced states. Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX. PLoS One 6 e27219 (2011)


Reviews citing this publication (1)

  1. The role of key residues in structure, function, and stability of cytochrome-c. Zaidi S, Hassan MI, Islam A, Ahmad F. Cell Mol Life Sci 71 229-255 (2014)

Articles citing this publication (4)

  1. Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action. Birth D, Kao WC, Hunte C. Nat Commun 5 4029 (2014)
  2. A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch. Amacher JF, Zhong F, Lisi GP, Zhu MQ, Alden SL, Hoke KR, Madden DR, Pletneva EV. J Am Chem Soc 137 8435-8449 (2015)
  3. Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics. Molano-Arevalo JC, Jeanne Dit Fouque K, Pham K, Miksovska J, Ridgeway ME, Park MA, Fernandez-Lima F. Anal Chem 89 8757-8765 (2017)
  4. Generation of novel functional metalloproteins via hybrids of cytochrome c and peroxidase. Ying T, Zhong F, Wang ZH, Xie J, Tan X, Huang ZX. Protein Eng Des Sel 26 401-407 (2013)


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