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Photosystem I

Photosystem I

Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...

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Related Experiment Video

Updated: Feb 5, 2026

Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film

Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film

Published on: July 10, 2016

InhA, the enoyl-thioester reductase from

Bastian Vögeli¹, Raoul G Rosenthal¹, Gabriele M M Stoffel¹

¹From the Departments of Biochemistry and Synthetic Metabolism and.

The Journal of Biological Chemistry

|September 16, 2018

Summary

Researchers discovered a covalent adduct formed during the enoyl-thioester reductase (InhA) reaction. This finding offers new insights into the InhA mechanism and aids in developing novel antituberculosis drugs.

Keywords:

InhA Mycobacterium tuberculosis enoyl-CoA reductase enzyme catalysis enzyme kinetics enzyme mechanism enzyme structure pericyclic reaction reductase short-chain dehydrogenase/reductase

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Last Updated: Feb 5, 2026

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Published on: September 7, 2011

Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Enoyl-thioester reductase (InhA) is crucial for Mycobacterium tuberculosis fatty acid biosynthesis.
InhA is a primary target for antituberculosis drugs, especially against multidrug-resistant strains.
Understanding the InhA reaction mechanism is vital for developing new therapeutic strategies.

Purpose of the Study:

To elucidate the catalytic mechanism and identify intermediates of the InhA reaction.
To investigate the roles of conserved active-site residues Tyr-158 and Thr-196.
To explore the implications of the InhA reaction mechanism for drug development.

Main Methods:

Enzyme mutagenesis
Nuclear Magnetic Resonance (NMR) spectroscopy
Stopped-flow spectroscopy
Liquid Chromatography-Mass Spectrometry (LC-MS)

Main Results:

A covalent adduct forms between the NADH cofactor and CoA thioester substrate during the InhA catalytic cycle.
This adduct allows independent study of the second half-reaction (proton transfer).
Tyr-158 is essential for stereospecific protonation, while Thr-196 participates in both hydride transfer and protonation.

Conclusions:

The formation of a covalent C2-ene adduct necessitates a re-evaluation of the InhA reaction mechanism.
Identified critical residues (Tyr-158, Thr-196) provide mechanistic insights.
Findings support the development of novel tools to study, manipulate, and inhibit InhA and related SDR enzymes for tuberculosis treatment.