Search Results - "Hargrove, Mark S."
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Plant hemoglobins: a journey from unicellular green algae to vascular plants
Published in The New phytologist (01-09-2020)“…Globins (Glbs) are widely distributed in archaea, bacteria and eukaryotes. They can be classified into proteins with 2/2 or 3/3 α-helical folding around…”
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2
Nitric oxide in plants: the roles of ascorbate and hemoglobin
Published in PloS one (20-12-2013)“…Ascorbic acid and hemoglobins have been linked to nitric oxide metabolism in plants. It has been hypothesized that ascorbic acid directly reduces plant…”
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Plant and Cyanobacterial Hemoglobins Reduce Nitrite to Nitric Oxide under Anoxic Conditions
Published in Biochemistry (Easton) (17-05-2011)“…The ability of ferrous hemoglobins to reduce nitrite to form nitric oxide has been demonstrated for hemoglobins from animals, including myoglobin, blood cell…”
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4
Structure and reactivity of hexacoordinate hemoglobins
Published in Biophysical chemistry (01-11-2010)“…The heme prosthetic group in hemoglobins is most often attached to the globin through coordination of either one or two histidine side chains. Those proteins…”
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NO dioxygenase activity in hemoglobins is ubiquitous in vitro, but limited by reduction in vivo
Published in PloS one (30-04-2008)“…Genomics has produced hundreds of new hemoglobin sequences with examples in nearly every living organism. Structural and biochemical characterizations of many…”
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6
A Ubiquitously Expressed Human Hexacoordinate Hemoglobin
Published in The Journal of biological chemistry (31-05-2002)“…We have identified a new human hemoglobin that we call histoglobin because it is expressed in a wide array of tissues. Histoglobin shares less than 30%…”
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7
Plant Hemoglobins: A Molecular Fossil Record for the Evolution of Oxygen Transport
Published in Journal of molecular biology (03-08-2007)“…The evolution of oxygen transport hemoglobins occurred on at least two independent occasions. The earliest event led to myoglobin and red blood cell hemoglobin…”
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8
Spectral, Kinetic, and Thermodynamic Properties of Cu(I) and Cu(II) Binding by Methanobactin from Methylosinus trichosporium OB3b
Published in Biochemistry (Easton) (07-02-2006)“…To examine the potential role of methanobactin (mb) as the extracellular component of a copper acquisition system in Methylosinus trichosporium OB3b, the metal…”
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9
Slow Ligand Binding Kinetics Dominate Ferrous Hexacoordinate Hemoglobin Reactivities and Reveal Differences between Plants and Other Species
Published in Biochemistry (Easton) (17-01-2006)“…Hexacoordinate hemoglobins are found in many living organisms ranging from prokaryotes to plants and animals. They are named “hexacoordinate” because of…”
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Comparison of the Dielectric Response Obtained from Fluorescence Upconversion Measurements and Molecular Dynamics Simulations for Coumarin 153−Apomyoglobin Complexes and Structural Analysis of the Complexes by NMR and Fluorescence Methods
Published in The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment, & general theory (28-04-2011)“…We present a comparison of the dielectric response obtained from fluorescence upconversion experiments and from molecular dynamics simulations of the complexes…”
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11
The role of the NADH-dependent nitrite reductase, Nir, from Escherichia coli in fermentative ammonification
Published in Archives of microbiology (01-05-2019)“…Nitrate and nitrite reduction are of paramount importance for nitrogen assimilation and anaerobic metabolism, and understanding the specific roles of each…”
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12
The Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage
Published in The Journal of biological chemistry (16-04-2004)“…The x-ray crystal structure of Synechocystis hemoglobin has been solved to a resolution of 1.8 Å. The conformation of this structure is surprisingly different…”
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13
Crystal structure of a nonsymbiotic plant hemoglobin
Published in Structure (London) (15-09-2000)“…Background: Nonsymbiotic hemoglobins (nsHbs) form a new class of plant proteins that is distinct genetically and structurally from leghemoglobins. They are…”
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Distal heme pocket regulation of ligand binding and stability in soybean leghemoglobin
Published in Proteins, structure, function, and bioinformatics (01-02-2003)“…Leghemoglobins facilitate diffusion of oxygen through root tissue to a bacterial terminal oxidase in much the same way that myoglobin transports oxygen from…”
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15
Crystallographic Analysis of Synechocystis Cyanoglobin Reveals the Structural Changes Accompanying Ligand Binding in a Hexacoordinate Hemoglobin
Published in Journal of molecular biology (20-08-2004)“…The crystal structures of cyanide and azide-bound forms of the truncated hemoglobin from Synechocystis are presented at 1.8 Å resolution. A comparison with the…”
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The Association Rate Constant for Heme Binding to Globin Is Independent of Protein Structure
Published in Biochemistry (Easton) (03-09-1996)“…Rate constants for CO-heme binding to 35 different recombinant apomyoglobins and several other apoproteins were measured in an effort to understand the factors…”
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Steady-State Kinetics of Phytoglobin-Catalyzed Reduction of Hydroxylamine to Ammonium
Published in Biochemistry (Easton) (14-08-2018)“…Phytoglobins are plant hexacoordinate hemoglobins with reversible coordination of a histidine side chain to the ligand binding site of the heme iron. They…”
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The Stability of Holomyoglobin Is Determined by Heme Affinity
Published in Biochemistry (Easton) (03-09-1996)“…The properties of wild-type, V68T, and H97D sperm whale myoglobins were compared to determine the relative importance of heme affinity and globin stability on…”
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Role of Reversible Histidine Coordination in Hydroxylamine Reduction by Plant Hemoglobins (Phytoglobins)
Published in Biochemistry (Easton) (18-10-2016)“…Reduction of hydroxylamine to ammonium by phytoglobin, a plant hexacoordinate hemoglobin, is much faster than that of other hexacoordinate hemoglobins or…”
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20
Oxygen Generation via Water Splitting by a Novel Biogenic Metal Ion-Binding Compound
Published in Applied and environmental microbiology (25-06-2021)“…Methanobactins (MBs) are small (<1,300-Da) posttranslationally modified copper-binding peptides and represent the extracellular component of a copper…”
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