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Related Concept Videos

Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Colors and Magnetism03:02

Colors and Magnetism

Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.
The Bohr Model02:18

The Bohr Model

Following the work of Ernest Rutherford and his colleagues in the early twentieth century, the picture of atoms consisting of tiny dense nuclei surrounded by lighter and even tinier electrons continually moving about the nucleus was well established. This picture was called the planetary model since it pictured the atom as a miniature “solar system” with the electrons orbiting the nucleus like planets orbiting the sun. The simplest atom is hydrogen, consisting of a single proton as the nucleus...
Hypoxia01:23

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...
Anoxygenic Photosynthesis01:30

Anoxygenic Photosynthesis

Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green sulfur bacteria, heliobacteria, and...

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Related Experiment Video

Updated: Jul 12, 2026

Measuring Photophysiology of Attached Stage of Colacium sp. by a Cuvette-Type Fast Repetition Rate Fluorometer
07:03

Measuring Photophysiology of Attached Stage of Colacium sp. by a Cuvette-Type Fast Repetition Rate Fluorometer

Published on: November 12, 2021

Bohr Effect: Absence in a Molluscan Hemocyanin.

J R Redmond

    Science (New York, N.Y.)
    |March 29, 1963
    PubMed
    Summary

    Keyhole limpet hemocyanin exhibits no Bohr effect, indicating stable oxygen binding across a pH range. Oxygenation involves positive cooperativity and releases significant heat.

    Area of Science:

    • Biochemistry
    • Marine Biology
    • Physiology

    Background:

    • Hemocyanins are copper-containing respiratory proteins in many marine invertebrates.
    • The Bohr effect describes the influence of pH on oxygen affinity in respiratory proteins.
    • Diodora aspera hemocyanin's physiological characteristics are not fully understood.

    Purpose of the Study:

    • To investigate the oxygen-binding properties of Diodora aspera hemocyanin.
    • To determine the presence and extent of the Bohr effect in this hemocyanin.
    • To characterize the thermodynamic and cooperativity aspects of oxygenation.

    Main Methods:

    • Oxygen equilibrium curves were measured for Diodora aspera hemocyanin.
    • Experiments were conducted across a defined pH range (6.88–7.84) and at a constant temperature (10°C).

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  • Thermodynamic parameters, including the heat of oxygenation, were calculated.

    • Main Results:

    • No significant Bohr effect was observed for Diodora aspera hemocyanin within the tested pH range.
    • The pressure of half-saturation (P50) was determined to be 5 mm-Hg at 10°C.
    • A moderately positive interaction (cooperativity) among oxygen-combining sites was detected during oxygenation.
    • The calculated heat of oxygenation was approximately -12.6 kcal/mole of oxygen.
    • The normal blood pH of Diodora aspera was found to be lower than that of many other marine molluscs.

    Conclusions:

    • Diodora aspera hemocyanin functions independently of pH changes within the physiological range studied.
    • The observed positive cooperativity suggests an allosteric mechanism for oxygen binding.
    • The significant negative heat of oxygenation indicates an exothermic binding process.
    • The lower blood pH may have implications for hemocyanin function and other physiological processes in Diodora aspera.