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A 192-heme electron transfer network in the hydrazine dehydrogenase complex

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Akram,  Mohd
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Dietl,  Andreas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Mersdorf,  Ulli
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Akram, M., Dietl, A., Mersdorf, U., Prinz, S., Maalcke, W. J., Keltjens, J. T., et al. (2019). A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Science Advances, 5(4): eaav4310, pp. 1-8. doi:10.1126/sciadv.aav4310.


Cite as: http://hdl.handle.net/21.11116/0000-0003-9F4E-4
Abstract
Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas andwater through the highly reactive intermediate hydrazine. So far, it is unknown how anammox organisms convert the toxic hydrazine into nitrogen and harvest the extremely low potential electrons (−750 mV) released in this process. We report the crystal structure and cryo electron microscopy structures of the responsible enzyme, hydrazine dehydrogenase, which is a 1.7MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way inwhich the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process.