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chemistry

Heme A

Heme A is a chemistry 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 Heme A rather than just read about it. In short: Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms.

Heme A — main illustration
Heme A — illustration

Key takeaways

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

Reference excerpt

Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood.

Relationship to other hemes Heme A differs from heme B in that a methyl side chain at ring position 8 is oxidized to a formyl group and a hydroxyethylfarnesyl group, an isoprenoid chain, has been attached to the vinyl side chain at ring position 2 of the iron tetrapyrrole heme. Heme A is similar to heme o, in that both have this farnesyl addition at position 2 but heme O does not have the formyl group at position 8, still containing the methyl group. The correct structure of heme A, based upon NMR and IR experiments of the reduced, Fe(II) form of the heme, was published in 1975. The structure was confirmed by synthesis of the dimethyl ester of the iron-free form.

History Heme A was first isolated by the German biochemist Otto Warburg in 1951 and shown by him to be the active component of the integral membrane metalloprotein cytochrome c oxidase.

Stereochemistry The final structural question of the exact geometric configuration about the first carbon at ring position 3 of ring I, the carbon bound to the hydroxyl group, has been shown to be the chiral S configuration. Like heme B, heme A is often attached to the apoprotein through a coordinate bond between the heme iron and a conserved amino acid side-chain. In the important respiratory protein cytochrome c oxidase (CCO) this ligand 5 for the heme A at the oxygen reaction center is a histidyl group. Histidine is a common ligand for many hemeproteins including hemoglobin and myoglobin.

Heme A in the cytochrome a portion of cytochrome c oxidase, bound by two histidine residues (shown in pink) An example of a metalloprotein that contains heme A is cytochrome c oxidase. This very complicated protein contains heme A at two different sites, each with a different function. The iron of the heme A of cytochrome a is hexacoordinated, that is bound with 6 other atoms. The iron of the heme A of cytochrome a3 is sometimes bound by 5 other atoms leaving the sixth site available to bind dioxygen (molecular oxygen). In addition, this enzyme binds 3 copper, magnesium, zinc, and several potassium and sodium ions. The two heme A groups in CCO are thought to readily exchange electrons between each other, the copper ions and the closely associated protein cytochrome c. Both the formyl group and the isoprenoid side chain are thought to play important roles in conservation of the energy of oxygen reduction by cytochrome c oxidase. CCO is thought to be responsible for conserving the energy of dioxygen reduction by pumping protons into the inter-membrane mitochondrial space. Both the formyl and hydroxyethylfarnesyl groups of heme A are thought to play important roles in this critical process, as published by the influential group of S. Yoshikawa.

See also Heme Hemoprotein Cytochrome c oxidase (Complex IV of cellular respiration)

References

Illustrations

Heme A illustration
Heme A illustration
Heme A illustration

Worked examples

Example 1 — a first encounter with Heme A

Start with the simplest possible case. Write down what Heme A claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In chemistry, 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 Heme A 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 Heme A 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 Heme A

In research
Heme A appears in chemistry 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 Heme A 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
Heme A is common in secondary-school and first-year university syllabi. It links to neighbouring topics Biomolecules, Tetrapyrroles, so understanding it makes those chapters shorter.
In everyday life
Look for Heme A 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 Heme A in 20 minutes

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

Frequently asked questions

What is Heme A in simple terms?

Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms.

Why does Heme A matter?

Because it connects several chemistry 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 Heme A?

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 Heme A.

Tags

  • Biomolecules
  • Tetrapyrroles

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