(Q27736382)

1

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A Galizzi

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A Coda

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P Ascenzi

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M Bolognesi

Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide

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publication date

15 April 1997

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published in

Structure

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volume

5

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issue

4

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page(s)

497-507

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cites work

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Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships

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7 January 2021

Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron

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Determinants of a protein fold. Unique features of the globin amino acid sequences

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The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases.

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Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states

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Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]

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Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases

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Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution

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Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron

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Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla

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Effect of Vitreoscilla hemoglobin dosage on microaerobic Escherichia coli carbon and energy metabolism

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Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o.

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The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases

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Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. Implications for protein function

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Presence of the bacterial hemoglobin gene improves alpha-amylase production of a recombinant Escherichia coli strain.

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Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin

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Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale

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Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus

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NADH-dependent methemoglobin reductase from the obligate aerobe Vitreoscilla: Improved method of purification and reexamination of prosthetic groups

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Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin at 1.78-A resolution. Phe29(B10) accounts for its unusual ligand binding properties

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Structural bases for sulfide recognition in Lucina pectinata hemoglobin I

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Engineering Ascaris hemoglobin oxygen affinity in sperm whale myoglobin: role of tyrosine B10

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THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN

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High-resolution crystallographic analysis of a co-operative dimeric hemoglobin

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Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola

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7 January 2021

Structural analysis of Urechis caupo hemoglobin

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Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria

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7 January 2021

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The locked rotation function

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