The atomic-resolution crystal structure of activated [Fe]-hydrogenase

Huang, Gangfeng; Wagner, T.; Wodrich, Matthew D.; Ataka, Kenichi; Bill, Eckhard; Ermler, Ulrich; Hu, Xile; Shima, Seigo

doi:10.1038/s41929-019-0289-4

Cited by 61 publications

(90 citation statements)

References 37 publications

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“…It is intriguing to notice that our proposal of a direct involvement of the Mo-bound oxo group in H 2 splitting finds a conceptually similar case in a recently published mechanistic study on the [Fe]-hydrogenase. In the latter enzyme, a deprotonared OH group that belongs to the iron-guanylylpyridinol cofactor and that is in γ-position with respect to the metal-activated H 2 , was suggested to be involved in substrate splitting [45]. Such mechanistic picture on the [Fe]-hydrogenase was the result of crystallographic studies that took advantage of the fact that the latter enzyme exists in two forms-an open substrate-accessible form and a closed catalytically active form.…”

Section: Discussionmentioning

confidence: 99%

Theoretical Insights into the Aerobic Hydrogenase Activity of Molybdenum–Copper CO Dehydrogenase

et al. 2019

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The Mo/Cu-dependent CO dehydrogenase from O. carboxydovorans is an enzyme that is able to catalyse CO oxidation to CO 2 ; moreover, it also expresses hydrogenase activity, as it is able to oxidize H 2 . Here, we have studied the dihydrogen oxidation catalysis by this enzyme using QM/MM calculations. Our results indicate that the equatorial oxo ligand of Mo is the best suited base for catalysis. Moreover, extraction of the first proton from H 2 by means of this basic centre leads to the formation of a Mo–OH–Cu I H hydride that allows for the stabilization of the copper hydride, otherwise known to be very unstable. In light of our results, two mechanisms for the hydrogenase activity of the enzyme are proposed. The first reactive channel depends on protonation of the sulphur atom of a Cu-bound cysteine residues, which appears to favour the binding and activation of the substrate. The second reactive channel involves a frustrated Lewis pair, formed by the equatorial oxo group bound to Mo and by the copper centre. In this case, no binding of the hydrogen molecule to the Cu center is observed but once H 2 enters into the active site, it can be split following a low-energy path.

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Section: Discussionmentioning

confidence: 99%

Theoretical Insights into the Aerobic Hydrogenase Activity of Molybdenum–Copper CO Dehydrogenase

et al. 2019

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“…[Fe]-hydrogenase [3] catalyzes the hydrogenation of methenyl-H 4 MPT + to methylene-H 4 MPT (H 4 MPT = tetrahydromethanopterin) with a complete stereospecificity and a high turnover frequency of up to 1900 s À1 (Figure 1 a). [4] The active site of [Fe]-hydrogenase comprises of a low-spin Fe II centre coordinated by one H 2 O and two cis-CO molecules, a cysteine thiolate, as well as an acyl carbon and a pyridinyl nitrogen from a guanylylpyridinol ligand (Figure 1 b). [4,5] The 2-OH group of the pyridonol ligand serves as an internal base to facilitate heterolytic H 2 activation upon deprotonation.…”

Section: Biomimetic Hydrogenation Catalyzed By a Manganese Model Of [mentioning

confidence: 99%

“…[4] The active site of [Fe]-hydrogenase comprises of a low-spin Fe II centre coordinated by one H 2 O and two cis-CO molecules, a cysteine thiolate, as well as an acyl carbon and a pyridinyl nitrogen from a guanylylpyridinol ligand (Figure 1 b). [4,5] The 2-OH group of the pyridonol ligand serves as an internal base to facilitate heterolytic H 2 activation upon deprotonation. [6] Many Fe complexes have been made to model the active site of [Fe]-hydrogenase.…”

Section: Biomimetic Hydrogenation Catalyzed By a Manganese Model Of [mentioning

confidence: 99%

Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]‐Hydrogenase

Pan

2020

Angew Chem Int Ed

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[Fe]‐hydrogenase is an efficient biological hydrogenation catalyst. Despite intense research, Fe complexes mimicking the active site of [Fe]‐hydrogenase have not achieved turnovers in hydrogenation reactions. Herein, we describe the design and development of a manganese(I) mimic of [Fe]‐hydrogenase. This complex exhibits the highest activity and broadest scope in catalytic hydrogenation among known mimics. Thanks to its biomimetic nature, the complex exhibits unique activity in the hydrogenation of compounds analogous to methenyl‐H4MPT+, the natural substrate of [Fe]‐hydrogenase. This activity enables asymmetric relay hydrogenation of benzoxazinones and benzoxazines, involving the hydrogenation of a chiral hydride transfer agent using our catalyst coupled to Lewis acid‐catalyzed hydride transfer from this agent to the substrates.

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“…[Fe]‐hydrogenase catalyzes the hydrogenation of methenyl‐H 4 MPT + to methylene‐H 4 MPT (H 4 MPT= tetrahydromethanopterin) with a complete stereospecificity and a high turnover frequency of up to 1900 s −1 (Figure a) . The active site of [Fe]‐hydrogenase comprises of a low‐spin Fe II centre coordinated by one H 2 O and two cis ‐CO molecules, a cysteine thiolate, as well as an acyl carbon and a pyridinyl nitrogen from a guanylylpyridinol ligand (Figure b) . The 2‐OH group of the pyridonol ligand serves as an internal base to facilitate heterolytic H 2 activation upon deprotonation …”

Section: Figurementioning

confidence: 99%