Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.

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Dynamic ruffling distortion of the heme substrate in non-canonical heme oxygenase enzymes.Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.

P2860

Q36044299-7BAEAC57-BAF3-4B1A-B38E-0D87AB543861 Q38840919-A390DD91-07E2-461F-8BDA-185A76367A6E

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Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.

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http://www.wikidata.org/entity/Q41015660

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Hydrogen bond donation to the ...... unes the electronic structure.

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type

Item

label

Hydrogen bond donation to the ...... unes the electronic structure.

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prefLabel

Hydrogen bond donation to the ...... unes the electronic structure.

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P1476

Hydrogen bond donation to the ...... tunes the electronic structure

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P2093

Cheryl L Lockhart

http://www.w3.org/2001/XMLSchema#string

Dylanger S Pittman

http://www.w3.org/2001/XMLSchema#string

Matthew D Liptak

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P2860

Community-associated methicillin-resistant Staphylococcus aureus: epidemiology and clinical consequences of an emerging epidemic

Generalized Gradient Approximation Made Simple

Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbon

Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuD

Ruffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureus

Unusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosis

The IsdG-family of haem oxygenases degrades haem to a novel chromophore

Inactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme Ruffling

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency

Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.

P2888

s00775-015-1263-5

P304

757-770

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P31

scholarly article

P356

10.1007/S00775-015-1263-5

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http://www.w3.org/2001/XMLSchema#string

P478

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Matthew A Conger

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2015-04-25T00:00:00Z

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P698

25911498

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Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.

about

P2860

P2860

Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.

description

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type

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P1433

P1476

P2093

P2860

P2888

P304

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P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698