Work

Hemoglobins dioxygenate nitric oxide with high fidelity

Year: 2006

Type: article

Source: Journal of Inorganic Biochemistry

DOI: 10.1016/j.jinorgbio.2005.12.012

Authors: Paul R. Gardner, Anne M. Gardner, Wayne T. Brashear, Tomohiko Suzuki, Angela N. Hvitved, Kenneth D.R. Setchell, John S. Olson

Institutions: Cincinnati Children's Hospital Medical Center, University of Kochi, Kōchi University, Rice University

Language: English

Topic: Hemoglobin structure and function

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: closed

Funders: National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences

Awards: Flavohemoglobin-catalyzed nitric oxide dioxygenation, G2154546777, Houston Area Molecular Biophysics Program, G3591803973, Functional Properties of Hemoglobins and Myoglobins, G678409930, Design of Heme Protein-Based Blood Substitutes

OpenAlex ID: W2086988804

FWCI: 3.167

Cites: 107

Cited by: 122

Related to: 10