Nitrosoamphetamine binding to myoglobin and hemoglobin: Crystal structure of the H64A myoglobin-nitrosoamphetamine adduct

Bing Wang, Samantha M. Powell, Ye Guan, Nan Xu, Leonard M. Thomas, George B. Richter-Addo

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

N-hydroxyamphetamine (AmphNHOH) is an oxidative metabolite of amphetamine and methamphetamine. It is known to form inhibitory complexes upon binding to heme proteins. However, its interactions with myoglobin (Mb) and hemoglobin (Hb) have not been reported. We demonstrate that the reactions of AmphNHOH with ferric Mb and Hb generate the respective heme-nitrosoamphetamine derivatives characterized by UV-vis spectroscopy. We have determined the X-ray crystal structure of the H64A Mb-nitrosoamphetamine complex to 1.73 Å resolution. The structure reveals the N-binding of the nitroso-d-amphetamine isomer, with no significant H-bonding interactions between the ligand and the distal pocket amino acid residues.

Original languageEnglish (US)
Pages (from-to)26-29
Number of pages4
JournalNitric Oxide - Biology and Chemistry
Volume67
DOIs
StatePublished - Jul 1 2017

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Clinical Biochemistry
  • Cancer Research

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