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deoxy hemerythrin and oxy hemerythrin

 3D View: Structure | Electron Density | Ligand Interaction, Biological assembly 1 assigned by authors and generated by PISA,PQS (software), Biological assembly 2 assigned by authors and generated by PISA (software), Biological assembly 3 generated by PQS (software), wwPDB Validation   3D Report Full Report. The deoxy form of hemerythrin is colorless, the oxy form is pink, and the met form is amber; this provides a simple visual check upon which form is present. See complete , THE STRUCTURE OF DEOXY AND OXY HEMERYTHRIN AT 2.0 ANGSTROMS RESOLUTION, National Institute of Allergy and Infectious Diseases, National Institute of General Medical Sciences, Primary Citation of Related Structures:  . RCSB PDB is funded by and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198. National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. NLM the US Department of Energy (DE-SC0019749), 2020 Jul;61(7):1104-1114. doi: 10.1194/jlr.RA120000803. Catalytic residues, substrate specificity, and role in carbon starvation of the 2-hydroxy FA dioxygenase Mpo1 in yeast. 2018 Mar 14;118(5):2554-2592. doi: 10.1021/acs.chemrev.7b00457. The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. Epub 2018 Feb 5.  |  The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom. Diffraction data were collected at the National Resource for Crystallography at the University of California, San Diego, CA, Dr N.-h. Xuong, Director. Clipboard, Search History, and several other advanced features are temporarily unavailable. Epub 2016 Dec 5. Restrained least-squares refinement has produced molecular models giving R-values of 16.8% for deoxy (41,064 reflections from 10 A to 2.0 A) and 17.3% for oxy hemerythrin (40,413 reflections from 10.0 A to 2.0 A). and the National Cancer Institute, 1988 Feb 9;27(3):1014-24. doi: 10.1021/bi00403a026. 2017 Aug 2;139(30):10472-10485. doi: 10.1021/jacs.7b05389. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom. HHS The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. J Biol Inorg Chem. Dioxygen binds to the pentaco-ordinate iron atom in deoxy hemerythrin in the conversion to oxy hemerythrin. Probing Hydrogen Bonding Interactions to Iron-Oxido/Hydroxido Units by. 2017 Apr;22(2-3):253-288. doi: 10.1007/s00775-016-1415-2. This is version 1.2 of the entry. Structures of met and azidomet hemerythrin at 1.66 A resolution. Weitz AC, Hill EA, Oswald VF, Bominaar EL, Borovik AS, Hendrich MP, Guo Y. Angew Chem Int Ed Engl. Nitric oxide adducts of the binuclear iron site of hemerythrin: spectroscopy and reactivity. Involvement of oxo-bridged binuclear iron centers in oxygen transport, oxygen reduction, and oxygenation. The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. The protein structure in each derivative is very similar to that of myohemerythrin and the various met forms of hemerythrin. Restrained least-squares refinement has produced molecular models giving R -values of 16.8% for deoxy (41,064 reflections from 10 Å to 2.0 Å) and 17.3% for oxy hemerythrin (40,413 reflections … Biochim Biophys Acta. Epub 2017 Jul 19. Activation of dioxygen by copper metalloproteins and insights from model complexes. National Institute of Allergy and Infectious Diseases, The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom. Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry. NIH Find NCBI SARS-CoV-2 literature, sequence, and clinical content: https://www.ncbi.nlm.nih.gov/sars-cov-2/. This work was supported by NIH grant GM-34663. 1991 Aug 5;220(3):723-37. doi: 10.1016/0022-2836(91)90113-k. Stenkamp RE, Sieker LC, Jensen LH, McCallum JD, Sanders-Loehr J. Proc Natl Acad Sci U S A. The crystallographic structure analyses of deoxy and oxy hemerythrin have been carried out at 2.0 A resolution to extend the low resolution views of the physiological forms of this oxygen-binding protein. The 2-0 A resolution data sets were collected rapidly to reduce possible conversion from deoxy to oxy and oxy to met forms. Copyright © 2020 Elsevier B.V. or its licensors or contributors. NCI CPTC Antibody Characterization Program. the bridging group is a hydroxyl. J Mol Biol. the bridging group is a hydroxyl. Active site structures of deoxyhemerythrin and oxyhemerythrin. Copyright © 1991 Published by Elsevier Ltd. https://doi.org/10.1016/0022-2836(91)90703-9.  |  Structures of deoxy and oxy hemerythrin at 2.0 Å resolution. The interatomic distances are consistent with the proposed mechanism where the proton from the bridging group is transferred to the bound dioxygen, stabilizing it in the peroxo oxidation state by forming a hydrogen bond between the peroxy group and the bridging oxygen atom.

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