Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels

Xiang Dong Tang, Rong Xu, Mark F. Reynolds, Maria L. Garcia, Stefan H. Heinemann and Toshinori Hoshi ()
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Xiang Dong Tang: University of Pennsylvania
Rong Xu: University of Pennsylvania
Mark F. Reynolds: Saint Joseph's University
Maria L. Garcia: Merck Research Laboratories
Stefan H. Heinemann: Medical Faculty of the Friedrich Schiller University Jena
Toshinori Hoshi: University of Pennsylvania

Nature, 2003, vol. 425, issue 6957, 531-535

Abstract: Abstract Haem is essential for living organisms, functioning as a crucial element in the redox-sensitive reaction centre in haemproteins1. During the biogenesis of these proteins, the haem cofactor is typically incorporated enzymatically into the haem pockets of the apo-haemprotein as the functionally indispensable prosthetic group2,3. A class of ion channel, the large-conductance calcium-dependent Slo1 BK channels, possesses a conserved haem-binding sequence motif. Here we present electrophysiological and structural evidence showing that haem directly regulates cloned human Slo1 channels and wild-type BK channels in rat brain. Both oxidized and reduced haem binds to the hSlo1 channel protein and profoundly inhibits transmembrane K+ currents by decreasing the frequency of channel opening. This direct regulation of the BK channel identifies a previously unknown role of haem as an acute signalling molecule.

Date: 2003
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DOI: 10.1038/nature02003

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