Explore the words cloud of the CaBiS project. It provides you a very rough idea of what is the project "CaBiS" about.
The following table provides information about the project.
|Coordinator Country||Sweden [SE]|
|Total cost||1˙494˙880 €|
|EC max contribution||1˙494˙880 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2017-02-01 to 2022-01-31|
Take a look of project's partnership.
|1||UPPSALA UNIVERSITET||SE (UPPSALA)||coordinator||1˙494˙880.00|
My proposal aims to take advantage of my ground-breaking finding that it is possible to mature, or activate, the [FeFe] hydrogenase enzyme (HydA) using synthetic mimics of its catalytic [2Fe] cofactor. (Berggren et al, Nature, 2013) We will now explore the chemistry and (bio-)technological potential of the enzyme using an interdisciplinary approach ranging from in vivo biochemical studies all the way to synthetic model chemistry. Hydrogenases catalyse the interconversion between protons and H2 with remarkable efficiency. Consequently, they are intensively studied as alternatives to Pt-catalysts for these reactions, and are arguably of high (bio-) technological importance in the light of a future “hydrogen society”. The project involves the preparation of novel “artificial” hydrogenases with the primary aim of designing spectroscopic model systems via modification(s) of the organometallic [2Fe] subsite. In parallel we will prepare in vitro loaded forms of the maturase HydF and study its interaction with apo-HydA in order to further elucidate the maturation process of HydA. Moreover we will develop the techniques necessary for in vivo application of the artificial activation concept, thereby paving the way for a multitude of studies including the reactivity of artificial hydrogenases inside a living cell, but also e.g. gain-of-function studies in combination with metabolomics and proteomics. Inspired by our work on the artificial maturation system we will also draw from our knowledge of Nature’s [FeS] cluster proteins in order to prepare a novel class of “miniaturized hydrogenases” combining synthetic [4Fe4S] binding oligopeptides with [2Fe] cofactor model compounds. Our interdisciplinary approach is particularly appealing as it not only provides further insight into hydrogenase chemistry and the maturation of metalloproteins, but also involves the development of novel tools and concepts applicable to the wider field of bioinorganic chemistry.
|year||authors and title||journal||last update|
LÃvia MÃ©szÃ¡ros, Pierre Ceccaldi, Marco Lorenzi, Holly Jayne Redman, Emanuel Pfitzner, Joachim Heberle, Moritz Senger, Sven Timo Stripp, Gustav Berggren
Spectroscopic investigations under whole cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase
published pages: , ISSN: 2041-6520, DOI: 10.1039/d0sc00512f
LÃvia S. MÃ©szÃ¡ros, Brigitta NÃ©meth, CharlÃ¨ne Esmieu, Pierre Ceccaldi, Gustav Berggren
Inâ€…Vivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases
published pages: 2596-2599, ISSN: 1433-7851, DOI: 10.1002/anie.201710740
|Angewandte Chemie International Edition 57/10||2019-06-13|
C. Esmieu, P. Raleiras, G. Berggren
From protein engineering to artificial enzymes â€“ biological and biomimetic approaches towards sustainable hydrogen production
published pages: 724-750, ISSN: 2398-4902, DOI: 10.1039/C7SE00582B
|Sustainable Energy & Fuels 2/4||2019-06-13|
N. Khanna, C. Esmieu, L. S. MÃ©szÃ¡ros, P. Lindblad, G. Berggren
In vivo activation of an [FeFe] hydrogenase using synthetic cofactors
published pages: 1563-1567, ISSN: 1754-5692, DOI: 10.1039/C7EE00135E
|Energy & Environmental Science 10/7||2019-06-13|
Brigitta NÃ©meth, CharlÃ¨ne Esmieu, Holly J. Redman, Gustav Berggren
Monitoring H-cluster assembly using a semi-synthetic HydF protein
published pages: 5978-5986, ISSN: 1477-9226, DOI: 10.1039/c8dt04294b
|Dalton Transactions 48/18||2019-08-29|
CharlÃ¨ne Esmieu, Meiyuan Guo, Holly J. Redman, Marcus Lundberg, Gustav Berggren
Synthesis of a miniaturized [FeFe] hydrogenase model system
published pages: 2280-2284, ISSN: 1477-9226, DOI: 10.1039/c8dt05085f
|Dalton Transactions 48/7||2019-08-29|
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