The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site. (Q30580749)

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11 December 2019

title

The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site (English)

1 reference

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Corynebacterium diphtheriae

11 December 2019

main subject

object named as

Corynebacterium diphtheriae

1 reference

2

1 reference

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11 December 2019

Frank D Sönnichsen

3

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11 December 2019

author name string

G C Chu

1

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11 December 2019

T Yoshida

4

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11 December 2019

M Ikeda-Saito

5

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11 December 2019

language of work or name

English

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publication date

1 August 1999

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Journal of Biological Chemistry

11 December 2019

published in

1 reference

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11 December 2019

volume

274

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11 December 2019

issue

35

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11 December 2019

page(s)

24490-24496

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Heme oxygenase 1 is required for mammalian iron reutilization

11 December 2019

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Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin

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Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle

21 January 2018

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Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae

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Probing axial ligands in ferric haemoproteins: An ESR study of myoglobin and horseradish peroxidase in H217O

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Heme-environment of horseradish peroxidase as observed by oxygen-17 superhyperfine interaction in EPR

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Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage

21 January 2018

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Assignment of exchangeable proximal histidine resonances in high-spin ferric hemoproteins: Substrate binding in horseradish peroxidase

21 January 2018

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Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1.

21 January 2018

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Proton NMR study of high-spin ferric natural porphyrin derivatives as models of methemoproteins

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Proton NMR hyperfine shift pattern as a probe for ligation state in high-spin ferric hemoproteins: water binding in metmyoglobin mutants

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Crystallization and preliminary X-ray diffraction analysis of a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae

21 January 2018

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Heme-heme oxygenase complex: structure and properties of the catalytic site from resonance Raman scattering

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Identification of histidine 25 as the heme ligand in human liver heme oxygenase

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Demonstration that histidine 25, but not 132, is the axial heme ligand in rat heme oxygenase-1

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