Histidine-834 of Human Erythrocyte Band 3 Has an Essential Role in the Conformational Changes That Occur during the Band 3-Mediated Anion Exchange

Xiu Ri Jin, Yoshito Abe, Chun Yan Li, Naotaka Hamasaki

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

We have shown that diethyl pyrocarbonate (DEPC) inhibits band 3-mediated anion exchange and that the inhibition occurs only when histidine residue(s) is (are) modified with DEPC from the cytosolic surface of resealed ghosts [Izuhara et al. (1989) Biochemistry 28, 4725-4728]. In the present study, we have identified the DEPC-modified histidine residue as His834 using liquid chromatography with electrospray ionization mass spectrometry (LC/ESI-MS). This mild, rapid, sensitive, and quantitative method was successfully applied to analysis of the unstable DEPC-histidine adduct. The DEPC modification of His834 was pH dependent and 4,4′-dinitrostilbene-2,2′-disulfonic acid (DNDS) sensitive as previously shown. After DEPC modification, band 3-mediated anion exchange is inhibited. Consistent with previous results, we confirmed that His834 was located on the cytosolic side of the membrane and the DEPC modification of His834 had allosteric effects on the extracellular DNDS-binding site of band 3. Therefore, we conclude that His834 is located at the cytosolic surface of band 3 and is an essential residue for band 3-mediated anion exchange. We will discuss important roles of the region from TM12 to TM14 in the conformational changes that occur during the band 3-mediated anion exchange.

Original languageEnglish
Pages (from-to)12927-12932
Number of pages6
JournalBiochemistry
Volume42
Issue number44
DOIs
Publication statusPublished - Nov 11 2003

All Science Journal Classification (ASJC) codes

  • Biochemistry

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