Strukturelle Interpretation metastabiler Zustände in Myoglobin‐NO

Soloviov, Maksym; Das, Akshaya Kumar; Meuwly, Markus

doi:10.1002/ange.201604552

Angewandte Chemie

2016

DOI: 10.1002/ange.201604552

|View full text |Cite

Strukturelle Interpretation metastabiler Zustände in Myoglobin‐NO

Maksym Soloviov¹,

Akshaya Kumar Das²,

Markus Meuwly³

Abstract: Die Bindung von Stickstoffmonoxid an Myoglobin (Mb) ist zentral für die Funktion des Proteins.M it reaktiven Moleküldynamiksimulationen wird die Dynamik nachd er NO-Dissoziation untersucht. Die NO-Rückbindung wird durch zwei Prozesse auf der 10-ps-und 100-ps-Zeitskala beschrieben, was mit Experimenten im optischen und Rçntgenbereich übereinstimmt. Dabei ist die explizite Behandlung der Bewegung des Eisenatoms orthogonal zur Häm-Ebene (Feoop) essenziell. Die Existenz eines transienten "Fe-oop/NOgebundenen" Zust… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2018

Publication Types

Select...

Article2

Relationship

Self Cite2

Independent0

Authors

Journals

Cited by 2 publications

References 43 publications

(66 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

Kinetische Analyse und strukturelle Interpretation der kompetitiven Ligandenbindung für Denitrifikation in gekürztem Hämoglobin N

Das¹,

Meuwly²

2018

Angewandte Chemie

Self Cite

View full text Add to dashboard Cite

Conversion of nitric oxide (NO) to nitrate (NO −3 ) by dioxygenation (NOD) protects cells from lethal NO. Starting from NO-bound heme, the first step in converting NO to benign NO − 3 is the ligand exchange reaction FeNO+O 2 → FeO 2 +NO which is still poorly understood at a molecular level. For WT truncated Hemoglobin N (trHbN) and its Y33A mutant the barrier for the exchange reaction differs by 1.5 kcal/mol compared with 1.7 kcal/mol from experiment. It is directly confirmed that the ligand exchange reaction is rate limiting in trHbN and that entropic contributions account for 75 % of the difference between WT and the mutant. Residues Tyr33, Phe46, Val80, His81and Gln82 surrounding the active site sample different ensembles in the ligand-bound and transition state (TS), respectively, and are expected to control the reaction path.Through comparison with electronic structure calculations the TS separating the two ligand-bound states is assigned to a 2 A state.

show abstract

Kinetische Analyse und strukturelle Interpretation der kompetitiven Ligandenbindung für Denitrifikation in gekürztem Hämoglobin N

Das¹,

Meuwly²

2018

Angewandte Chemie

Self Cite

View full text Add to dashboard Cite

show abstract

Kinetic Analysis and Structural Interpretation of Competitive Ligand Binding for NO Dioxygenation in Truncated Hemoglobin N

Das

Meuwly

2018

Angew Chem Int Ed

Self Cite

View full text Add to dashboard Cite

The conversion of nitric oxide (NO) into nitrate (NO ) by dioxygenation protects cells from lethal NO. Starting from NO-bound heme, the first step in converting NO into benign NO is the ligand exchange reaction FeNO+O →FeO +NO, which is still poorly understood at a molecular level. For wild-type (WT) truncated hemoglobin N (trHbN) and its Y33A mutant, the calculated barriers for the exchange reaction differ by 1.5 kcal mol , compared with 1.7 kcal mol from experiment. It is directly confirmed that the ligand exchange reaction is rate-limiting in trHbN and that entropic contributions account for 75 % of the difference between the WT and the mutant. Residues Tyr 33, Phe 46, Val 80, His 81, and Gln 82 surrounding the active site are expected to control the reaction path. By comparison with electronic structure calculations, the transition state separating the two ligand-bound states was assigned to a A state.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Strukturelle Interpretation metastabiler Zustände in Myoglobin‐NO

Cited by 2 publications

References 43 publications

Kinetische Analyse und strukturelle Interpretation der kompetitiven Ligandenbindung für Denitrifikation in gekürztem Hämoglobin N

Kinetische Analyse und strukturelle Interpretation der kompetitiven Ligandenbindung für Denitrifikation in gekürztem Hämoglobin N

Kinetic Analysis and Structural Interpretation of Competitive Ligand Binding for NO Dioxygenation in Truncated Hemoglobin N

Contact Info

Product

Resources

About