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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…
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Keywords:
hemoglobin;
spectrin;
heme proteins;
spectrin binding ... See more keywords
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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…
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Keywords:
heme;
heme proteins;
proteins using;
using hybrid ... See more keywords
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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…
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Keywords:
heme;
heme proteins;
function heme;
structure function ... See more keywords
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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,…
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Keywords:
complexity;
bond;
heme proteins;
biology ... See more keywords
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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…
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Keywords:
drug;
heme proteins;
proteins mycobacterium;
targeting heme ... See more keywords
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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…
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Keywords:
heme;
oligomerization cytochrome;
heme proteins;
proteins domain ... See more keywords
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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…
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Keywords:
heme proteins;
carbene nitrene;
carbene;
nitrene transfer ... See more keywords
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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…
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Keywords:
production;
heme;
escherichia coli;
heme proteins ... See more keywords
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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…
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Keywords:
femtosecond stimulated;
heme;
stimulated raman;
heme proteins ... See more keywords
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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.…
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Keywords:
spectroscopy;
heme proteins;
heme;
resonance raman ... See more keywords
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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…
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Keywords:
peroxynitrite detoxification;
heme;
detoxification ferric;
heme proteins ... See more keywords