4M4A

Human Hemoglobin Nitromethane Modified

Summary for 4M4A

• Entry DOI: 10.2210/pdb4m4a/pdb
• Related: 4M4B
• Descriptor: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: r-state, human hemoglobin, nitromethane modified, oxygen transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 32639.89

Authors

Yi, J.,Guan, Y.,Thomas, L.M.,Richter-Addo, G.B. (deposition date: 2013-08-06, release date: 2014-07-16, Last modification date: 2023-09-20)

Primary citation

Yi, J.,Ye, G.,Thomas, L.M.,Richter-Addo, G.B.
Degradation of human hemoglobin by organic C-nitroso compounds.
Chem.Commun.(Camb.), 49:11179-11181, 2013

PubMed Abstract: The crystal structure of the nitrosomethane adduct of human Hb shows N-binding of the MeNO ligands to heme Fe. The structure of the EtNO adduct reveals a surprising 4.9 Å heme slippage in the β subunit, and explains the ability of C-nitroso compounds to degrade Hb removing it from circulation.

PubMed: 24149619
DOI: 10.1039/c3cc46174b

Experimental method

X-RAY DIFFRACTION (2.05 Å)