Articles with "heme proteins" as a keyword



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Erythroid spectrin binding modulates peroxidase and catalase activity of heme proteins.

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Published in 2022 at "IUBMB life"

DOI: 10.1002/iub.2607

Abstract: Hemoglobin oxidation due to oxidative stress and disease conditions leads to generation of ROS (reactive oxygen species) and membrane attachment of hemoglobin in-vivo, where its redox activity leads to peroxidative damage of membrane lipids and… read more here.

Keywords: hemoglobin; spectrin; heme proteins; spectrin binding ... See more keywords
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Exploring the folding energy landscapes of heme proteins using a hybrid AWSEM-heme model

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Published in 2022 at "Journal of Biological Physics"

DOI: 10.1007/s10867-021-09596-3

Abstract: Heme is an active center in many proteins. Here we explore computationally the role of heme in protein folding and protein structure. We model heme proteins using a hybrid model employing the AWSEM Hamiltonian, a… read more here.

Keywords: heme; heme proteins; proteins using; using hybrid ... See more keywords
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Structure and function of heme proteins regulated by diverse post-translational modifications.

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Published in 2018 at "Archives of biochemistry and biophysics"

DOI: 10.1016/j.abb.2018.01.009

Abstract: Heme proteins are crucial for biological systems by performing diverse functions. Nature has evolved diverse approaches to fine-tune the structure and function of heme proteins, of which post-translational modification (PTM) is a primary method. As… read more here.

Keywords: heme; heme proteins; function heme; structure function ... See more keywords
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Selective CH bond functionalization with engineered heme proteins: new tools to generate complexity.

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Published in 2019 at "Current opinion in chemical biology"

DOI: 10.1016/j.cbpa.2018.10.004

Abstract: CH functionalization is an attractive strategy to construct and diversify molecules. Heme proteins, predominantly cytochromes P450, are responsible for an array of CH oxidations in biology. Recent work has coupled concepts from synthetic chemistry, computation,… read more here.

Keywords: complexity; bond; heme proteins; biology ... See more keywords
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Drug targeting of heme proteins in Mycobacterium tuberculosis.

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Published in 2017 at "Drug discovery today"

DOI: 10.1016/j.drudis.2016.11.004

Abstract: TB, caused by the human pathogen Mycobacterium tuberculosis (Mtb), causes more deaths than any other infectious disease. Iron is crucial for Mtb to infect the host and to sustain infection, with Mtb encoding large numbers… read more here.

Keywords: drug; heme proteins; proteins mycobacterium; targeting heme ... See more keywords
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Oligomerization of cytochrome c, myoglobin, and related heme proteins by 3D domain swapping.

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Published in 2019 at "Journal of inorganic biochemistry"

DOI: 10.1016/j.jinorgbio.2019.03.002

Abstract: Oligomerization of heme proteins is useful for construction of new materials with cooperative and systematic functions; thus, diverse methods have been applied for construction of artificial heme protein oligomers. Three-dimensional (3D) domain swapping is a… read more here.

Keywords: heme; oligomerization cytochrome; heme proteins; proteins domain ... See more keywords
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Navigating the Unnatural Reaction Space: Directed Evolution of Heme Proteins for Selective Carbene and Nitrene Transfer.

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Published in 2021 at "Accounts of chemical research"

DOI: 10.1021/acs.accounts.0c00591

Abstract: ConspectusDespite the astonishing diversity of naturally occurring biocatalytic processes, enzymes do not catalyze many of the transformations favored by synthetic chemists. Either nature does not care about the specific products, or if she does, she… read more here.

Keywords: heme proteins; carbene nitrene; carbene; nitrene transfer ... See more keywords
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Improved Method for the Incorporation of Heme Cofactors into Recombinant Proteins Using Escherichia coli Nissle 1917.

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Published in 2018 at "Biochemistry"

DOI: 10.1021/acs.biochem.8b00242

Abstract: Recombinant production of heme proteins in Escherichia coli is often limited by the availability of heme in the host. Therefore, several methods, including the reconstitution of heme proteins after production but prior to purification or… read more here.

Keywords: production; heme; escherichia coli; heme proteins ... See more keywords
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Ultrafast Dynamics and Vibrational Relaxation in Six-Coordinate Heme Proteins Revealed by Femtosecond Stimulated Raman Spectroscopy

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Published in 2020 at "Journal of the American Chemical Society"

DOI: 10.1021/jacs.9b10560

Abstract: Identifying the structural rearrangements during photoinduced reactions is a fundamental challenge for understanding from a microscopic perspective the dynamics underlying the functional mechanisms of heme proteins. Here, femtosecond stimulated Raman spectroscopy is applied to follow… read more here.

Keywords: femtosecond stimulated; heme; stimulated raman; heme proteins ... See more keywords
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Solution and crystal phase resonance Raman spectroscopy: Valuable tools to unveil the structure and function of heme proteins

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Published in 2019 at "Journal of Porphyrins and Phthalocyanines"

DOI: 10.1142/s1088424619300088

Abstract: In the present review, examples are provided illustrating the application of resonance Raman microscopy to heme protein single crystals to highlight the artifacts induced by the crystallization process or the conformational alteration induced by cooling.… read more here.

Keywords: spectroscopy; heme proteins; heme; resonance raman ... See more keywords
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The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO2: The Case of Zebrafish Nitrobindin

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Published in 2022 at "Antioxidants"

DOI: 10.3390/antiox11101932

Abstract: Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric Danio rerio… read more here.

Keywords: peroxynitrite detoxification; heme; detoxification ferric; heme proteins ... See more keywords