[H₀] Conventional symbol historically used for the constant magnetic field in an MR system; it is physically more correct to use B0.

[H₁] H1 is a conventional symbol historically used for the radio frequency magnetic field related to MRI; today B1 is in use.

See B1.

(Hb) Haemoglobin is the major endogenous oxygen-binding molecule, responsible for binding oxygen in the lung and transporting it to the tissues by means of the circulation. Haemoglobin is contained in very high concentration in the red blood cells.
Haemoglobin is an Fe chelate tightly binding one Fe ion in its II oxidation state where it carries the charge 2+ (ferrous iron). If an oxygen molecule is bound to Hb, Hb is called oxyhaemoglobin, if no oxygen molecule is bound it is called deoxyhaemoglobin. When haemoglobin is oxidized (i.e. in a haematoma), Fe2+ is transformed into Fe3+. The resulting haemoglobin is then called metoxyhaemoglobin (Hb Fe3+).
Deoxyhaemoglobin and metoxyhaemoglobin act as paramagnetic contrast agents in MR, while oxyhaemoglobin is diamagnetic. This partly explains the special appearance of an aging haematoma in MR imaging and is also the basic of the blood oxygenation level dependent contrast (BOLD) used in functional magnetic resonance imaging of the brain (fMRI).

After a bleeding, blood goes through several transitions regarding magnetic properties, intra- and extracellular distribution and content of proteins and water. Oxyhaemoglobin is degraded to deoxyhaemoglobin and further to methaemoglobin, ferritin and haemosiderin. These molecules can be characterized by their magnetic susceptibility effect. Oxyhaemoglobin is diamagnetic with no practical influence on the magnetic field. All degradation products are paramagnetic (deoxyhaemoglobin, methaemoglobin) or even superparamagnetic (ferritin, haemosiderin).

See also Haemoglobin, Blood Oxygenation Level Dependent Contrast.

Production of spin echo by repeated RF pulses. First observed using equal (90°) RF pulses, now commonly used to describe refocusing of transverse magnetization by a 180° RF pulse. By choosing long echo delay times, the spins in a Hahn echo first dephase for a long time, then rephase, which makes the Hahn pulse sequence more susceptible to diffusion effects.