engineering

Hydrogen:quinone oxidoreductase

Hydrogen:quinone oxidoreductase is a engineering topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Hydrogen:quinone oxidoreductase rather than just read about it. In short: In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction H2 + quinone ⇌ {\displaystyle \rightleftharpoons } quinol Thus, the two substrates of this enzyme are H2 and quinone, whereas its product is quinol. The quinone can be menaquinone, ubiquinone, demethylmenaquinone or methionaquinone.

Key takeaways

Hydrogen:quinone oxidoreductase belongs to engineering; place it in that map before memorising details.
Learn the definition first, then one example that makes the definition concrete.
Connect Hydrogen:quinone oxidoreductase to a quantity you can measure, compute or draw — that is where exam questions come from.
Reproduce the core statement of Hydrogen:quinone oxidoreductase from memory before moving on to harder problems.

Reference excerpt

In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction

H2 + quinone ⇌ {\displaystyle \rightleftharpoons } quinol Thus, the two substrates of this enzyme are H2 and quinone, whereas its product is quinol. The quinone can be menaquinone, ubiquinone, demethylmenaquinone or methionaquinone. This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a quinone or similar compound as acceptor. The systematic name of this enzyme class is hydrogen:quinone oxidoreductase. Other names in common use include hydrogen-ubiquinone oxidoreductase, hydrogen:menaquinone oxidoreductase, membrane-bound hydrogenase, and quinone-reactive Ni/Fe-hydrogenase.

References

E, Duchene A, Tripier D, Juvenal K, et al. (1992). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes". Eur. J. Biochem. 206 (1): 93–102. doi:10.1111/j.1432-1033.1992.tb16905.x. PMID 1587288. E, Duchene A, Tripier D, Juvenal K, et al. (1993). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella Succinogenes". Eur. J. Biochem. 214 (3): 949–50. doi:10.1111/j.1432-1033.1993.tb17999.x. PMID 8319698. Gross R, Simon J, Lancaster CR, Kröger A (1998). "Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2". Mol. Microbiol. 30 (3): 639–46. doi:10.1046/j.1365-2958.1998.01100.x. PMID 9822828. Bernhard M, Benelli B, Hochkoeppler A, Zannoni D, Friedrich B (1997). "Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16". Eur. J. Biochem. 248 (1): 179–86. doi:10.1111/j.1432-1033.1997.00179.x. PMID 9310376. Ferber DM, Maier RJ (1993). "Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase". FEMS Microbiol. Lett. 110 (3): 257–64. doi:10.1111/j.1574-6968.1993.tb06331.x. PMID 8354459. Kodama T (1991). "Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6". Agric. Biol. Chem. 55 (12): 3011–3016. doi:10.1271/bbb1961.55.3011. Infossi, Pascale; Lojou, Elisabeth; Chauvin, Jean-Paul; Herbette, Gaetan; Brugna, Myriam; Giudici-Orticoni, Marie-Thérèse (2010). "Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: Role of lipids and physiological partners in enzyme stability and activity". International Journal of Hydrogen Energy. 35 (19): 10778–10789. Bibcode:2010IJHE...3510778I. doi:10.1016/j.ijhydene.2010.02.054. ISSN 0360-3199. Frielingsdorf, Stefan; Schubert, Torsten; Pohlmann, Anne; Lenz, Oliver; Friedrich, Bärbel (2011). "A Trimeric Supercomplex of the Oxygen-Tolerant Membrane-Bound [NiFe]-Hydrogenase fromRalstonia eutrophaH16". Biochemistry. 50 (50): 10836–10843. doi:10.1021/bi201594m. ISSN 0006-2960. Radu, Valentin; Frielingsdorf, Stefan; Evans, Stephen D.; Lenz, Oliver; Jeuken, Lars J. C. (2014). "Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase ofRalstonia eutropha". Journal of the American Chemical Society. 136 (24): 8512–8515. Bibcode:2014JAChS.136.8512R. doi:10.1021/ja503138p. ISSN 0002-7863. PMC 4073834. PMID 24866391.

Worked examples

Example 1 — a first encounter with Hydrogen:quinone oxidoreductase

Start with the simplest possible case. Write down what Hydrogen:quinone oxidoreductase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In engineering, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Hydrogen:quinone oxidoreductase before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Hydrogen:quinone oxidoreductase ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Hydrogen:quinone oxidoreductase

In research: Hydrogen:quinone oxidoreductase appears in engineering research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Hydrogen:quinone oxidoreductase in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Hydrogen:quinone oxidoreductase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 1.12.5, Enzymes of unknown structure, Oxidoreductase stubs, so understanding it makes those chapters shorter.
In everyday life: Look for Hydrogen:quinone oxidoreductase outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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How to study Hydrogen:quinone oxidoreductase in 20 minutes

Read the reference excerpt below once, without taking notes.
Close the page and write down what Hydrogen:quinone oxidoreductase means in your own words.
Compare your version with the excerpt and mark what you missed.
Work through the three examples above with pen and paper.
Explain Hydrogen:quinone oxidoreductase out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Hydrogen:quinone oxidoreductase in simple terms?

In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction H2 + quinone ⇌ {\displaystyle \rightleftharpoons } quinol Thus, the two substrates of this enzyme are H2 and quinone, whereas its product is quinol. The quinone can be menaquinone, ubiqu…

Why does Hydrogen:quinone oxidoreductase matter?

Because it connects several engineering ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Hydrogen:quinone oxidoreductase?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Hydrogen:quinone oxidoreductase.