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Colors and Magnetism03:02

Colors and Magnetism

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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...
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Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

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Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the involved orbitals. The...
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Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)01:20

Spin–Spin Coupling: Two-Bond Coupling (Geminal Coupling)

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Two NMR-active nuclei bonded to a central atom can be involved in geminal or two-bond coupling. Geminal coupling is commonly seen between diastereotopic protons in chiral molecules and unsymmetrical alkenes, among others.
The central atom need not be NMR-active because its electrons are affected by the electron polarization of the spin-active atoms. However, spin information is transmitted less effectively than in one-bond coupling, and 2J values are usually weaker than 1J values. The energy of...
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Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

1.5K
Coupling interactions are strongest between NMR-active nuclei bonded to each other, where spin information can be transmitted directly through the pair of bonding electrons. While nuclei polarize their electrons to the opposite spins, the bonding electron pair has opposite spins. Configurations with antiparallel nuclear spins are expected to be lower in energy. When coupling makes antiparallel states more favorable, J is considered to have a positive value. The one-bond coupling constant, 1J,...
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Redox Equilibria: Overview01:23

Redox Equilibria: Overview

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A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.4K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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Related Experiment Video

Updated: Mar 3, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

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Secondary-Sphere Hydrogen Bonds Regulating Spin-Redox Interplay in Hemes.

Subhadip Pramanik1, Chengxu Zhu2,3, Paulami Chakraborty1

  • 1Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur, India.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 2, 2026
PubMed
Summary

Hydrogen bonding significantly impacts heme enzyme function by altering iron

Keywords:
Fe(III)PorphyrinH‐bondingredox potentialspin flippingstructure elucidation

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EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
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EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
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Area of Science:

  • Bioinorganic Chemistry
  • Computational Chemistry
  • Biophysical Chemistry

Background:

  • Hydrogen bonding (H-bonding) is crucial for metalloprotein function, influencing substrate binding and active-site geometry.
  • In heme enzymes, H-bonding networks modulate iron's redox potentials and spin states, impacting catalytic efficiency.
  • The precise molecular origins of H-bonding effects on heme electronic structure and redox properties require further exploration.

Purpose of the Study:

  • To investigate the influence of secondary-sphere H-bonding interactions on the geometry, spin state, and redox properties of iron(III) porphyrin complexes.
  • To elucidate the molecular mechanisms by which H-bonding regulates heme electronic structure and redox behavior.
  • To provide fundamental insights into enzymatic regulation through H-bonding.

Main Methods:

  • Synthesis and characterization of iron(III) porphyrin-phenoxide and iron(III)-chloro complexes.
  • Spectroscopic analysis (e.g., UV-Vis, EPR) to determine spin states and structural parameters.
  • Electrochemical studies (e.g., cyclic voltammetry) to probe redox potentials.
  • Computational modeling (e.g., DFT calculations) to support experimental findings.

Main Results:

  • Secondary-sphere H-bonding elongated the axial Fe─O bond and contracted the porphyrin core in iron(III) porphyrin-phenoxide complexes.
  • H-bonding stabilized the intermediate-spin (S = 3/2) state, while its absence favored the high-spin (S = 5/2) state.
  • Electrochemical studies showed positive shifts in Fe(III)/Fe(II) redox potentials and 1e- oxidation upon H-bonding, indicating redox noninnocence.

Conclusions:

  • Secondary-sphere H-bonding significantly influences the geometry, spin state, and redox properties of heme iron centers.
  • H-bonding acts as a key regulator of redox noninnocence in heme systems.
  • These findings offer fundamental insights into the role of H-bonding in enzymatic catalysis and regulation.