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Open AccessJournal ArticleDOI

The H93G Myoglobin Cavity Mutant as a Versatile Scaffold for Modeling Heme Iron Coordination Structures in Protein Active Sites and Their Characterization with Magnetic Circular Dichroism Spectroscopy.

TLDR
The use of magnetic circular dichroism and electronic absorption spectroscopy is reviewed to characterize nitrogen-, oxygen-, and sulfur-donor-ligated H93G Mb adducts with an emphasis on species not easily prepared by other heme model system approaches and those that serve as spectroscopic models for native heme proteins.
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This article is published in Coordination Chemistry Reviews.The article was published on 2011-04-01 and is currently open access. It has received 50 citations till now. The article focuses on the topics: Heme & Hemeprotein.

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Rational design of metalloenzymes: From single to multiple active sites

TL;DR: This review summarizes the recent achievements in rational design of metalloenzymes from single to multiple active sites in natural or de novo protein scaffolds, with a diverse range of functionalities, even beyond those of natural metall Koenzymes.
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The Mycobacterium tuberculosis secreted protein Rv0203 transfers heme to membrane proteins MmpL3 and MmpL11.

TL;DR: MmpL3 and MmpL11 are potential heme transporters, whereby heme is transported into the cytosol, as elucidates a key step in the mycobacterial uptake of heme, and it may be useful in the development of anti-tuberculosis drugs targeting this pathway.
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Structure and function of heme proteins regulated by diverse post-translational modifications.

TL;DR: The tremendous progress made in research methods and advances in research techniques will make it possible to rationally control the diverse PTMs of heme proteins, especially those associated with human diseases, toward the authors' desired goals for a better life.
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Structural and oxygen binding properties of dimeric horse myoglobin

TL;DR: It is found that dimeric metMb exhibits a domain-swapped structure with two extended α-helices, and results show that domain swapping may be a new tool for protein engineering.
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Role of Met80 and Tyr67 in the low-pH conformational equilibria of cytochrome c.

TL;DR: Data show that removal of the axial methionine ligand does not significantly alter the mechanism of acidic unfolding and the ranges of stability of low-pH conformers, and underlines the key role played by Tyr67 in stabilizing the three-dimensional structure of cytochrome c by means of the hydrogen bonding network connecting the Ω loops formed by residues 71-85 and 40-57.
References
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Book

Cytochrome P-450: Structure, Mechanism, and Biochemistry

TL;DR: The Cytochrome P450 and the Metabolism and Bioactivation of Arachidonic Acid and Eicosanoids in Plants and the Diversity and Importance of Microbial Cytochromes P450 are studied.
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High-resolution three-dimensional structure of horse heart cytochrome c.

TL;DR: This study demonstrates that, in horse cytochrome c, the side-chain of Phe82 is positioned in a co-planar fashion next to the heme in a conformation comparable to that found in other cytochromes c, and strongly implicates this internal water molecule as having a functional role in the mechanism of action of cy tochrome c.
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Probing structure-function relations in heme-containing oxygenases and peroxidases

TL;DR: Structural factors that influence functional properties are examined in the case of four heme enzymes and the importance of synthetic porphyrin models in understanding the properties of the protein-free metal center is emphasized.
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