{"id":120500,"date":"2023-01-06T07:29:00","date_gmt":"2023-01-06T06:29:00","guid":{"rendered":"https:\/\/renewable-carbon.eu\/news\/?p=120500"},"modified":"2023-01-03T13:17:18","modified_gmt":"2023-01-03T12:17:18","slug":"a-poison-helps-to-understand-h2-producing-biocatalysts","status":"publish","type":"post","link":"https:\/\/renewable-carbon.eu\/news\/a-poison-helps-to-understand-h2-producing-biocatalysts\/","title":{"rendered":"A poison helps to understand H2-producing biocatalysts"},"content":{"rendered":"\n

<\/h2>\n\n\n\n\n\n
\"\nThomas
Thomas Happe is researching biocatalysts that can produce hydrogen in an environmentally friendly way.
\u00a9\u00a0RUB, Marquard<\/figcaption><\/figure><\/div>\n\n\n\n

In nature, enzymes termed hydrogenases are capable of producing molecular hydrogen (H2<\/sub>). Special types of these biocatalysts, so-called [FeFe]-hydrogenases, are extremely efficient and therefore of interest for biobased hydrogen production. Although scientists have learned a lot about how these enzymes work, many details remain to be completely understood. A research team of the Photobiotechnology group at Ruhr University Bochum, Germany, headed by Dr. Jifu Duan and Professor Thomas Happe succeeded in filling a scientific gap. The researchers showed that external cyanide binds to the [FeFe] hydrogenases and inhibits hydrogen formation. In the process, they detected a structural change in the proton transport pathway, which helps to understand the coupling of electron and proton transport. They reported their findings in the journal \u201cAngewandte Chemie\u201d<\/a> of 4 December 2022.<\/strong><\/p>\n\n\n\n

A sophisticated internal catalyst<\/h4>\n\n\n\n

To generate H2<\/sub>, these biocatalysts transfer electrons to protons, employing a sophisticated structure as internal catalyst. This so-called H-cluster contains electronically active iron ions that are bound to what most people know as toxins: carbon monoxide and cyanide. However, although internal carbon monoxide and cyanide are crucial for the high activity of hydrogenases, additional external carbon monoxide binds to the H-cluster and prevents its H2<\/sub>\u00a0production. <\/p>\n\n\n\n

\u201cInterestingly, cyanide is also a well-known inhibitor of iron-containing biocatalysts,\u201d says Jifu Duan<\/strong>. \u201cAnd yet, its effect on [FeFe]-hydrogenases has hardly been analysed before.\u201d<\/p><\/blockquote>\n\n\n\n

\"Thomas
Thomas Happe, Jifu Duan, Eckhard Hofmann and Anja Hemschemeier (from left) represent the team of authors.\u00a9\u00a0RUB, Marquard<\/figcaption><\/figure><\/div>\n\n\n\n

The Bochum-based research team closed this scientific gap. The researchers showed that external cyanide binds to and inhibits [FeFe]-hydrogenases. In collaboration with Professor Eckhard Hofmann, head of the protein crystallography group at RUB, the team obtained the structure of H2<\/sub>-producing biocatalysts to which external cyanide was bound. <\/p>\n\n\n\n

\u201cThe high-resolution structure in combination with spectroscopic analyses tells us that the external cyanide directly binds to the H-cluster, similar to other inhibitors studied so far,\u201d says Jifu Duan<\/strong>. \u201cThis explains why the hydrogenase is inactive after cyanide treatment.\u201d<\/p><\/blockquote>\n\n\n\n

Coincidental capture of a transient state<\/h4>\n\n\n\n

When the researchers took a detailed look into the structure of the cyanide-poisoned hydrogenase, they found a surprise. They observed structural changes in the proton transport pathway that is required to guide the protons that will become H2<\/sub>to the H-cluster. <\/p>\n\n\n\n

\u201cThis conformation has been suggested to be vital for efficient proton shuttling, but it had never been observed structurally. Coincidently, the cyanide binding helped us to capture such a transient state\u201d, says Jifu Duan<\/strong>. \u201cThese findings are important for researchers to understand the coupling of electron and proton transport which is not only relevant for H2<\/sub>-generating enzymes, but many additional biocatalysts,\u201d concludes Thomas Happe<\/strong>.<\/p><\/blockquote>\n\n\n\n

Funding<\/h3>\n\n\n\n

The researchers received financial support from Deutsche Forschungsgemeinschaft, VolkswagenStiftung and Germany\u2019s Excellence Strategy \u2013 EXC 2033 (Project number 390677874).<\/p>\n\n\n\n

Original publication<\/h3>\n\n\n\n

Jifu Duan, Anja Hemschemeier, David J. Burr, Sven T. Stripp, Eckhard Hofmann, Thomas Happe: Cyanide binding to [FeFe]-hydrogenase stabilizes the alternative configuration of the proton transfer pathway, Angewandte Chemie, 2022, DOI:\u00a010.1002\/anie.202216903<\/a><\/strong><\/p>\n\n\n\n

Contacts<\/h3>\n\n\n\n

Prof. Dr. Thomas Happe
Photobiotechnology Group
Department of Plant Biochemistry
Faculty for Biology and Biotechnology
Phone: +49 234 32 27026
Email:\u00a0thomas.happe@rub.de<\/a><\/p>\n\n\n\n

Dr. Jifu Duan
Photobiotechnology Group
Department of Plant Biochemistry
Faculty for Biology and Biotechnology
Phone: +49 234 32 24496
Email:\u00a0jifu.duan@rub.de<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

In nature, enzymes termed hydrogenases are capable of producing molecular hydrogen (H2). Special types of these biocatalysts, so-called [FeFe]-hydrogenases, are extremely efficient and therefore of interest for biobased hydrogen production. Although scientists have learned a lot about how these enzymes work, many details remain to be completely understood. A research team of the Photobiotechnology group […]<\/p>\n","protected":false},"author":59,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_seopress_robots_primary_cat":"none","nova_meta_subtitle":"The toxic cyanide molecule attacks H2-generating enzymes, but at the same time provides new insights into catalysis","footnotes":""},"categories":[5572],"tags":[11833,5796,5840,10630],"supplier":[1806],"class_list":["post-120500","post","type-post","status-publish","format-standard","hentry","category-bio-based","tag-biocatalysis","tag-biotechnology","tag-enzymes","tag-hydrogen","supplier-ruhr-universitaet-bochum"],"_links":{"self":[{"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/posts\/120500","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/users\/59"}],"replies":[{"embeddable":true,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/comments?post=120500"}],"version-history":[{"count":0,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/posts\/120500\/revisions"}],"wp:attachment":[{"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/media?parent=120500"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/categories?post=120500"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/tags?post=120500"},{"taxonomy":"supplier","embeddable":true,"href":"https:\/\/renewable-carbon.eu\/news\/wp-json\/wp\/v2\/supplier?post=120500"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}