Andreas Rutz's research while affiliated with Ruhr-Universität Bochum and other places
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Publications (7)
The high turnover rates of [FeFe]-hydrogenases under mild conditions and at low overpotentials provide a natural blueprint for the design of hydrogen catalysts. However, the unique active site (H-cluster) degrades upon contact with oxygen. The [FeFe]-hydrogenase fromClostridium beijerinckii (CbA5H) is characterized by the flexibility of its protein...
Correction for ‘The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal’ by Melanie Heghmanns et al. , Chem. Sci. , 2022, 13 , 7289–7294, https://doi.org/10.1039/D2SC00385F.
[FeFe]-hydrogenases catalyze the reversible conversion of molecular hydrogen into protons and electrons with remarkable efficiency. However, their industrial applications are limited by their oxygen sensitivity. Recently, it was shown that the [FeFe]-hydrogenase from Clostridium beijerinckii (CbA5H) is oxygen-resistant and can be reactivated after...
![The unusual O2-resistance of [FeFe]-hydrogenase CbA5H
The H-cluster of...](profile/Jifu-Duan/publication/348971994/figure/fig3/AS:987778523340801@1612516160605/The-unusual-O2-resistance-of-FeFe-hydrogenase-CbA5H-The-H-cluster-of-CpI-and-other_Q320.jpg)
FeFe]-hydrogenases are efficient H 2-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-transform infrared spectroscopy to describe a protein morphing mechanism that controls the reversible t...
Gaining knowledge about the algal hydrogen metabolism is prerequisite for the biotechnological exploitation of photosynthetic H2 production. Model organism Chlamydomonas reinhardtii encodes two [FeFe]-hydrogenases, which are individually capable of catalysing the reversible reduction of protons to molecular hydrogen. While physiological results ind...
Significance
The maturation of each hydrogenase class describes the process that converts an apo-hydrogenase into an active holoenzyme involving a machinery of maturases. For [FeFe]-hydrogenases, the synthesis and insertion of the catalytic dinuclear [2Fe H ]-cofactor is executed by the 3 maturases (HydE, HydF, and HydG) that have already been stud...
Citations
... [FeFe]-hydrogenases are under further investigation using spectroscopic techniques to understand the mechanisms of O 2 tolerance. Kasanmascheff et al. reported an interesting radical (R •ox ) in the [FeFe]-hydrogenase CbA5H, which is known to be O 2 -tolerant [87,138]. When kept under aerobic conditions, the R •ox signal significantly increases while CbA5H remains in the Hinact state. ...
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... This hints at H 2 O 2 as a key ROS in the deactivation process. The structure of the H-cluster in the O 2 -inhibited state Hinact of DdHydAB and CbA5H was debatted until crystallographic analyses revealed that a cysteine residue binds to Fe d of the H-cluster, protecting the cofactor from O 2 deactivation like a 'safety cap' [87]. Interestingly, sulfide has a similar effect and binds to Fe d under oxidizing conditions both aerobic and anaerobic (Fig. 5), which allows reversible conversion of the Hox and Hinact states [88][89][90]. ...
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... H 2 production and relative expression of hyd and fdx in C. vulgaris, S. obliquus, and C. reinhardtii HYD and FDX are proteins that are characterized by the presence of Fe 2 S 2 centers, which is important for the oxidationreduction reactions of these enzymes (Mulder et al. 2010;Ohnishi et al. 2020;Engelbrecht et al. 2021). The incubation in periods of darkness and subsequent exposure to light has been reported to have an impact on H 2 production and on the regulation of HYD in algae (Yang et al. 2013;Weiner et al. 2018;Subramanian et al. 2019;Li et al. 2020). ...
... Structural studies of the [FeFe]-hydrogenase maturation process are few, but Happe et al. have shown that incorporation of the [2Fe] H cluster is guided by arginine R449 and lysine L358 of CpI [140]. The molecular backbone movements could be studied by dipolar-dipolar EPR spectroscopy, e.g., between the H-cluster and a nitroxide label or between multiple nitroxide labels that have been incorporated by site-directed mutagenesis [141]. ...
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