Functional aspects of ultra-rapid heme doming in hemoglobin, myoglobin, and the myoglobin mutant H93G (Q72428598)

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26 October 2019

title

Functional aspects of ultra-rapid heme doming in hemoglobin, myoglobin, and the myoglobin mutant H93G (English)

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26 October 2019

5

S G Boxer

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26 October 2019

author name string

S Franzen

1

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26 October 2019

B Bohn

2

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26 October 2019

C Poyart

3

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26 October 2019

G DePillis

4

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26 October 2019

J L Martin

6

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26 October 2019

language of work or name

English

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publication date

1 January 1995

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Journal of Biological Chemistry

26 October 2019

number of pages

3

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based on heuristic

inferred from page(s)

published in

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26 October 2019

volume

270

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26 October 2019

issue

4

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26 October 2019

page(s)

1718-1720

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Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

26 October 2019

cites work

1 reference

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Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly

21 January 2018

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Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity.

21 January 2018

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Direct evidence for the role of haem doming as the primary event in the cooperative transition of haemoglobin

21 January 2018

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Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin

21 January 2018

1 reference

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Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity

21 January 2018

1 reference

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Assignment of the Fe-Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin

21 January 2018

1 reference

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Temperature dependence of the structure and dynamics of myoglobin. A simulation approach

21 January 2018

1 reference

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Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant

21 January 2018

1 reference

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

21 January 2018

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Molecular description of dioxygen bonding in hemoglobin

21 January 2018

1 reference

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

21 January 2018

1 reference

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Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme

21 January 2018

1 reference

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Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change

21 January 2018

1 reference

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Real time observation of low frequency heme protein vibrations using femtosecond coherence spectroscopy

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.4.1718

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7829506%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

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